Showing drug card for L-Cysteine (DB00151)

• NUTR00018

• Approved
• Nutraceutical
• Small Molecule

1. (R)-2-Amino-3-mercaptopropanoic acid
2. (R)-Cysteine
3. 2-Amino-3-mercaptopropionic acid
4. 3-mercapto-L-Alanine
5. Cys
6. Cystein
7. Half-cystine
8. L-(+)-Cysteine
9. L-2-Amino-3-mercaptopropionic acid
10. L-Cys
11. Thioserine
12. b-Mercaptoalanine
13. carbocysteine

1. Amino Acid Concentrate Inj (Arginine Hcl + Calcium Chloride + Dexpanthenol + Dextrose + Dl-Methionine + Glutamic Acid + Histidine Hcl + Isoleucine + L-Cysteine Hydrochloride + L-Lysine Hydrochloride + Leucine + Magnesium Sulfate + Nicotinamide + Phenylalanine + Potassium Chloride + Sodium Acetate + Threonine + Tryptophan + Valine + Vitamin B1 (Thiamine) + Vitamin B12 + Vitamin B2 (Riboflavin) + Vitamin B6 (Pyridoxine))
2. Amino Acid Inj (Arginine + Calcium Chloride + D-Pantothenic Acid (Calcium D-Pantothenate) + Dextrose + Histidine + Isoleucine + L-Cysteine Hydrochloride + Leucine + Lysine + Magnesium Sulfate + Methionine + Nicotinamide + Phenylalanine + Potassium Chloride + Pyridoxine Hydrochloride + Sodium Acetate + Threonine + Tryptophan + Valine + Vitamin B1 + Vitamin B12 + Vitamin B2)
3. Amino Lite (Arginine + Calcium Chloride + Dextrose + Isoleucine + L-Cysteine Hydrochloride + L-Histidine Hcl + L-Lysine Hydrochloride + Leucine + Magnesium Sulfate + Methionine + Nicotinic Acid + Phenylalanine + Potassium Chloride + Pyridoxine Hydrochloride + Sodium Glutamate + Thiamine Hydrochloride + Threonine + Tryptophan + Valine + Vitamin B12 + Vitamin B2 (Riboflavin 5'-Phosphate Sodium))
4. Aminoderm Poudre (Glycine + L-Cysteine + Neomycin Sulfate + Threonine)
5. Bvs Amino Acid Solution Inj (Arginine Hcl + Calcium Chloride + Dexpanthenol + Dextrose + Dl-Isoleucine + L-Cysteine Hydrochloride + L-Histidine Hcl + L-Lysine Hydrochloride + Leucine + Magnesium Sulfate + Methionine + Nicotinamide + Phenylalanine + Potassium Chloride + Pyridoxine Hydrochloride + Sodium Acetate Hemodialysis + Sodium Glutamate + Threonine + Tryptophan + Valine + Vitamin B1 + Vitamin B12 + Vitamin B2)
6. Cicatrin Powder (Bacitracin Zinc + Glycine + L-Cysteine + Neomycin Sulfate + Threonine)
7. Nephramine Liq Iv (Dl-Methionine + Histidine + Isoleucine + L-Cysteine (L-Cysteine Hydrochloride) + Leucine + Lysine (Lysine Acetate) + Phenylalanine + Sodium Bisulfite + Threonine + Tryptophan + Valine)
8. Primene 10% (Glutamic Acid + Glycine + Histidine + L-Alanine + L-Arginine + L-Aspartic Acid + L-Cysteine + L-Isoleucine + L-Leucine + L-Lysine + L-Ornithine Dihydrochloride + L-Phenylalanine + L-Proline + L-Threonine + L-Tyrosine + L-Valine + Methionine + Serine + Taurine + Tryptophan)
9. Primene 10%-Liq Iv (Glutamic Acid + Glycine + Histidine + L-Alanine + L-Arginine + L-Aspartic Acid + L-Cysteine Hydrochloride + L-Isoleucine + L-Leucine + L-Lysine + L-Ornithine + L-Phenylalanine + L-Proline + L-Threonine + L-Tyrosine + L-Valine + Methionine + Serine + Taurine + Tryptophan)
10. Stv Amino Acid Sol Inj (Arginine Hcl + Calcium Chloride + Dexpanthenol + Dextrose + Dl-Methionine + Glutamic Acid + Histidine Hcl + Isoleucine + L-Cysteine Hydrochloride + L-Lysine Hydrochloride + Leucine + Magnesium Sulfate + Nicotinamide + Phenylalanine + Potassium Chloride + Pyridoxine Hydrochloride + Sodium Acetate + Threonine + Tryptophan + Valine + Vitamin B1 (Thiamine) + Vitamin B12 + Vitamin B2 (Riboflavin))
11. Vamin 18 Electrolyte-Free (Glutamic Acid + Glycine + Histidine + L-Alanine + L-Arginine + L-Aspartic Acid + L-Cysteine + L-Isoleucine + L-Leucine + L-Lysine (Lysine Acetate) + L-Phenylalanine + L-Proline + L-Threonine + L-Tyrosine + L-Valine + Methionine + Serine + Tryptophan)
12. Vamin N (Calcium Chloride + Glutamic Acid + Glycine + Histidine + L-Alanine + L-Arginine + L-Aspartic Acid + L-Cysteine (L-Cysteine Hydrochloride) + L-Isoleucine + L-Leucine + L-Lysine (L-Lysine Hydrochloride) + L-Phenylalanine + L-Proline + L-Threonine + L-Tyrosine + L-Valine + Magnesium Sulfate + Methionine + Potassium Chloride + Potassium Hydroxide + Serine + Sodium Hydroxide + Tryptophan)

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• Dietary supplement
• Nutritional Supplement

• R05CB01
• S01XA08
• V03AB23

1. Baker DH, Czarnecki-Maulden GL: Pharmacologic role of cysteine in ameliorating or exacerbating mineral toxicities. J Nutr. 1987 Jun;117(6):1003-10. [PubMed ]
2. Bulaj G, Kortemme T, Goldenberg DP: Ionization-reactivity relationships for cysteine thiols in polypeptides. Biochemistry. 1998 Jun 23;37(25):8965-72. [PubMed ]
3. Wikipedia

• Humans and other mammals

1. Cysteine sulfinic acid decarboxylase
2. Cysteine desulfurase, mitochondrial
3. Cysteine dioxygenase
4. Glutamate--cysteine ligase catalytic subunit
5. Glutathione synthetase
6. Cystathionine beta-synthase
7. Aspartate aminotransferase, cytoplasmic
8. Cysteine dioxygenase type 1
9. Glutamate--cysteine ligase regulatory subunit
10. Cysteinyl-tRNA synthetase, cytoplasmic
11. Cystathionine gamma-lyase
12. Thiamine transporter 2
13. Methylated-DNA--protein-cysteine methyltransferase
14. Probable cysteinyl-tRNA synthetase, mitochondrial

1. Cysteine-sulfinate decarboxylase
2. EC 4.1.1.29
3. Sulfinoalanine decarboxylase

MADSEALPSLAGDPVAVEALLRAVFGVVVDEAIQKGTSVSQKVCEWKEPEELKQLLDLEL
RSQGESQKQILERCRAVIRYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEI
APVFVLMEEEVLRKLRALVGWSSGDGIFCPGGSISNMYAVNLARYQRYPDCKQRGLRTLP
PLALFTSKECHYSIQKGAAFLGLGTDSVRVVKADERGKMVPEDLERQIGMAEAEGAVPFL
VSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHRHLLDGIQRADSVA
WNPHKLLAAGLQCSALLLQDTSNLLKRCHGSQASYLFQQDKFYDVALDTGDKVVQCGRRV
DCLKLWLMWKAQGDQGLERRIDQAFVLARYLVEEMKKREGFELVMEPEFVNVCFWFVPPS
LRGKQESPDYHERLSKVAPVLKERMVKEGSMMIGYQPHGTRGNFFRVVVANSALTCADMD
FLLNELERLGQDL

• 3-sulfino-L-alanine = hypotaurine + CO2

• Pyridoxal_deC (PF00282 )

• None

• None

ATGGCTGACTCAGAAGCACTCCCCTCCCTTGCTGGGGACCCAGTGGCTGTGGAAGCCTTG
CTCCGGGCCGTGTTTGGGGTTGTTGTGGATGAGGCCATTCAGAAAGGAACCAGTGTCTCC
CAGAAGGTCTGTGAGTGGAAGGAGCCTGAGGAGCTGAAGCAGCTGCTGGATTTGGAGCTG
CGGAGCCAGGGCGAGTCACAGAAGCAGATCCTGGAGCGGTGTCGGGCTGTGATTCGCTAC
AGTGTCAAGACTGGTCACCCTCGGTTCTTCAACCAGCTCTTCTCTGGGTTGGATCCCCAT
GCTCTGGCCGGGCGCATTATCACTGAGAGCCTCAACACCAGCCAGTACACATATGAAATC
GCCCCCGTGTTTGTGCTCATGGAAGAGGAGGTGCTGAGGAAACTGCGGGCCCTGGTGGGC
TGGAGCTCTGGGGACGGAATCTTCTGCCCTGGTGGCTCCATCTCCAACATGTATGCTGTA
AATCTGGCCCGCTATCAGCGCTACCCGGATTGCAAGCAGAGGGGCCTCCGCACACTGCCG
CCCCTGGCCCTATTCACATCGAAGGAGTGTCACTACTCCATCCAGAAGGGAGCTGCGTTT
CTGGGACTTGGCACCGACAGTGTCCGAGTGGTCAAGGCTGATGAGAGAGGGAAAATGGTC
CCCGAGGATCTGGAGAGGCAGATTGGTATGGCCGAGGCTGAGGGTGCTGTGCCGTTCCTG
GTCAGTGCCACCTCTGGCACCACTGTGCTAGGGGCCTTTGACCCCCTGGGGGCAATTGCT
GATGTGTGCCAGCGTCATGGGCTATGGCTGCATGTGGATGCTGCCTGGGGTGGGAGCGTC
CTGCTGTCACAGACACACAGGCATCTCCTGGATGGGATCCAGAGGGCTGACTCTGTGGCC
TGGAATCCCCACAAGCTCCTCGCAGCAGGCCTGCAATGCTCTGCACTTCTTCTCCAGGAT
ACCTCGAACCTGCTCAAGCGCTGCCATGGGTCCCAGGCCAGCTACCTTTTCCAGCAGGAC
AAGTTCTACGATGTGGCTCTGGACACGGGAGACAAGGTGGTGCAGTGTGGCCGCCGTGTG
GACTGTCTGAAGCTGTGGCTCATGTGGAAGGCACAGGGCGATCAAGGGCTGGAGCGGCGC
ATCGACCAGGCCTTTGTCCTTGCCCGGTACCTGGTGGAGGAAATGAAGAAGCGGGAAGGG
TTTGAGCTAGTCATGGAGCCTGAGTTTGTCAATGTGTGTTTCTGGTTCGTACCCCCCAGC
CTGCGAGGGAAGCAGGAGAGTCCAGATTACCACGAAAGGCTGTCAAAGGTGGCCCCCGTG
CTCAAGGAGCGCATGGTGAAGGAGGGCTCCATGATGATTGGCTACCAGCCCCACGGGACC
CGGGGCAACTTCTTCCGTGTGGTTGTGGCCAACTCTGCACTGACCTGTGCTGATATGGAC
TTCCTCCTCAACGAGCTGGAGCGGCTAGGCCAGGACCTGTGA

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]
3. Guion-Rain M-C, Portemer C, Chatagner F: Rat liver cysteine sulfinate decarboxylase: purification, new appraisal of the molecular weight and determination of catalytic properties. Biochim Biophys Acta. 1975 Mar 28;384(1):265-76. [PubMed ]
4. Chan-Palay V, Lin CT, Palay S, Yamamoto M, Wu JY: Taurine in the mammalian cerebellum: demonstration by autoradiography with [3H]taurine and immunocytochemistry with antibodies against the taurine-synthesizing enzyme, cysteine-sulfinic acid decarboxylase. Proc Natl Acad Sci U S A. 1982 Apr;79(8):2695-9. [PubMed ]
5. Daniels KM, Stipanuk MH: The effect of dietary cysteine level on cysteine metabolism in rats. J Nutr. 1982 Nov;112(11):2130-41. [PubMed ]

1. Cysteine desulfurase, mitochondrial precursor
2. EC 2.8.1.7

MLLRAAWRRAAVAVTAAPGPKPAAPTRGLRLRVGDRAPQSAVPADTAAAPEVGPVLRPLY
MDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPRE
IIFTSGATESNNIAIKGVARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQK
SGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGRICSSRKVYFHTDAAQAVGKI
PLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVPTPL
VVGLGAACEVAQQEMEYDHKRISKLSERLIQNIMKSLPDVVMNGDPKHHYPGCINLSFAY
VEGESLLMALKDVALSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVD
YTVEKCIQHVKRLREMSPLWEMVQDGIDLKSIKWTQH

• L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine ALL_REAC (other) R07460

• Aminotran_5 (PF00266 )

• None

• None

• Mitochondrion. Cytoplasm

ATGCTGCTCCGAGTCGCTTGGAGGCGGGCGGCAGTGGCGGTGACAGCGGCTCCAGGGCCG
AAGCCCGCGGCGCCCACTCGGGGGCTGCGCCTGCGCGTTGGAGACCGTGCTCCTCAGTCT
GCGGTTCCCGCAGATACAACCGCTGCCCCGGAGGTGGGGCCAGTGCTGCGACCTCTCTAT
ATGGATGTGCAAGCTACAACTCCTCTGGACCCCCGGGTGCTTGATGCCATGCTCCCTTAC
CTAATCAACTACTATGGGAACCCACACTCCCGGACACATGCTTATGGCTGGGAGAGTGAG
GCAGCCATGGAACGTGCTCGTCAGCAAGTAGCATCTCTGATTGGAGCTGATCCTCGTGAG
ATCATTTTTACTAGTGGTGCTACTGAATCCAACAACATAGCAATTAAGGGGGTGGCCCGA
TTCTACAGGTCACGGAAAAAGCACTTGATCACCACCCAGACAGAACACAAATGTGTCTTG
GACTCCTGCCGTTCACTGGAAGCTGAGGGCTTTCAGGTCACCTACCTCCCAGTGCAGAAG
AGTGGGATCATTGACCTAAAGGAACTAGAGGCTGCTATCCAGCCAGATACTAGCCTGGTG
TCAGTCATGACTGTGAACAATGAGATTGGAGTGAAGCAGCCTATTGCAGAAATAGGGCGG
ATTTGCAGTTCCAGAAAGGTATATTTCCATACTGATGCAGCCCAGGCTGTTGGAAAAATC
CCACTTGATGTCAATGACATGAAAATTGATCTCATGAGCATTAGTGGTCACAAAATCTAC
GGTCCCAAAGGGGTTGGTGCCATCTACATCCGTCGCCGGCCCCGTGTGCGTGTGGAGGCC
CTGCAGAGTGGAGGGGGGCAGGAGCGGGGTATGCGGTCTGGGACAGTGCCCACACCCTTA
GTGGTGGGGTTGGGGGCTGCGTGTGAGGTGGCACAGCAAGAGATGGAGTATGACCACAAG
CGAATCTCAAAGTTGTCAGAGCGGCTGATACAGAATATAATGAAGAGCCTTCCAGATGTG
GTGATGAATGGGGACCCTAAGCACCATTATCCCGGCTGTATCAACCTCTCCTTTGCATAT
GTGGAAGGGGAAAGTCTGCTGATGGCACTGAAGGACGTTGCCTTATCCTCAGGGAGTGCC
TGCACCTCTGCATCCCTGGAGCCCTCTTATGTGCTTAGAGCAATTGGCACTGATGAGGAT
TTAGCGCACTCTTCTATCAGGTTTGGAATTGGCGCTTTCACTACAGAGGAGGAAGTGGAC
TACACAGTGGAGAAATGCATTCAGCATGTGAATCGTCTTCGAGAAATGAGCCCTCTCTGG
GAGATGGTTCAGGATGGCATTGACCTCAAGAGCATCAAGTGGACCCAACACTAG

1. Tong WH, Rouault T: Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells. EMBO J. 2000 Nov 1;19(21):5692-700. [PubMed ]
2. Stanchi F, Bertocco E, Toppo S, Dioguardi R, Simionati B, Cannata N, Zimbello R, Lanfranchi G, Valle G: Characterization of 16 novel human genes showing high similarity to yeast sequences. Yeast. 2001 Jan 15;18(1):69-80. [PubMed ]
3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed ]
4. Land T, Rouault TA: Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization. Mol Cell. 1998 Dec;2(6):807-15. [PubMed ]

1. Ding B, Smith ES, Ding H: Mobilization of the iron centre in IscA for the iron-sulphur cluster assembly in IscU. Biochem J. 2005 Aug 1;389(Pt 3):797-802. [PubMed ]
2. Ding H, Harrison K, Lu J: Thioredoxin reductase system mediates iron binding in IscA and iron delivery for the iron-sulfur cluster assembly in IscU. J Biol Chem. 2005 Aug 26;280(34):30432-7. Epub 2005 Jun 28. [PubMed ]
3. Layer G, Ollagnier-de Choudens S, Sanakis Y, Fontecave M: Iron-sulfur cluster biosynthesis: characterization of Escherichia coli CYaY as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU. J Biol Chem. 2006 Jun 16;281(24):16256-63. Epub 2006 Apr 9. [PubMed ]
4. Yang J, Bitoun JP, Ding H: Interplay of IscA and IscU in biogenesis of iron-sulfur clusters. J Biol Chem. 2006 Sep 22;281(38):27956-63. Epub 2006 Jul 27. [PubMed ]
5. You D, Wang L, Yao F, Zhou X, Deng Z: A novel DNA modification by sulfur: DndA is a NifS-like cysteine desulfurase capable of assembling DndC as an iron-sulfur cluster protein in Streptomyces lividans. Biochemistry. 2007 May 22;46(20):6126-33. Epub 2007 May 1. [PubMed ]

1. EC 1.13.11.20

MEQTEVLKPRTLADLIRILHQLFAGDEVNVEEVQAIMEAYESDPIEWAMYAKFDQY

• L-cysteine + O2 = 3-sulfinoalanine

• CDO_I (PF05995 )

• None

• None

ATGGAACAGACCGAAGTGCTGAAGCCACGGACCCTGGCTGATCTGATCCGCATCCTGCAC
CAGCTCTTTGCCGGCGATGAGGTCAATGTAGAGGAGGTGCAGGCCATCATGGAAGCCTAC
GAGAGCGACCCCATCGAGTGGGCAATGTACGCCAAGTTCGACCAGTACAGGTATACCCGA
AATCTTGTGGATCAAGGAAATGGAAAATTTAATCTGATGATTCTCTGTTGGGGTGAAGGA
CATGGCAGCAGTATTCATGATCATACCAACTCCCACTGCTTTCTGAAGATGCTACAGGGA
AATCTAAAGGAGACATTATTTGCCTGGCCTGACAAAAAATCCAATGAGATGGTCAAGAAG
TCTGAAAGAGTCTTGAGGGAAAACCAGTGTGCCTACATCAATGATTCCATTGGCTTACAT
CGAGTAGAGAACATCAGCCATACGGAACCTGCTGTGAGCCTTCACTTGTACAGTCCACCT
TTTGATACATGCCATGCCTTTGATCAAAGAACAGGACATAAAAACAAAGTCACAATGACA
TTCCATAGTAAATTTGGAATCAGAACTCCAAATGCAACTTCGGGCTCGCTGGAGAACAAC
TAA

1. Roopnarinesingh ES, Steventon GB, Harris RM, Waring RH, Mitchell SC: Induction of cysteine dioxygenase activity by oral administration of cysteine analogues to the rat: implications for drug efficacy and safety. Drug Metabol Drug Interact. 2005;21(2):75-86. [PubMed ]
2. McCoy JG, Bailey LJ, Bitto E, Bingman CA, Aceti DJ, Fox BG, Phillips GN Jr: Structure and mechanism of mouse cysteine dioxygenase. Proc Natl Acad Sci U S A. 2006 Feb 28;103(9):3084-9. Epub 2006 Feb 21. [PubMed ]
3. Ye S, Wu X, Wei L, Tang D, Sun P, Bartlam M, Rao Z: An insight into the mechanism of human cysteine dioxygenase. Key roles of the thioether-bonded tyrosine-cysteine cofactor. J Biol Chem. 2007 Feb 2;282(5):3391-402. Epub 2006 Nov 29. [PubMed ]
4. Pierce BS, Gardner JD, Bailey LJ, Brunold TC, Fox BG: Characterization of the nitrosyl adduct of substrate-bound mouse cysteine dioxygenase by electron paramagnetic resonance: electronic structure of the active site and mechanistic implications. Biochemistry. 2007 Jul 24;46(29):8569-78. Epub 2007 Jun 28. [PubMed ]
5. Jin HF, DU SX, Zhao X, Zhang SQ, Tian Y, Bu DF, Tang CS, DU JB: [Significance of endogenous sulfur dioxide in the regulation of cardiovascular system] Beijing Da Xue Xue Bao. 2007 Aug 18;39(4):423-5. [PubMed ]

1. EC 6.3.2.2
2. GCS heavy chain
3. Gamma- glutamylcysteine synthetase
4. Gamma-ECS

GLLSQGSPLSWEETKRHADHVRRHGILQFLHIYHAVKDRHKDVLKWGDEVEYMLVSFDHE
NKKVRLVLSGEKVLETLQEKGERTNPNHPTLWRPEYGSYMIEGTPGQPYGGTMSEFNTVE
ANMRKRRKEATSILEENQALCTITSFPRLGCPGFTLPEVKPNPVEGGASKSLFFPDEAIN
KHPRFSTLTRNIRHRRGEKVVINVPIFKDKNTPSPFIETFTEDDEASRASKPDHIYMDAM
GFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVIS
ASVDDRTREERGLEPLKNNNYRISKSRYDSIDSYLSKCGEKYNDIDLTIDKEIYEQLLQE
GIDHLLAQHVAHLFIRDPLTLFEEKIHLDDANESDHFENIQSTNWQTMRFKPPPPNSDIG
WRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMKVAQKRDAVLQ
GMFYFRKDICKGGNAVVDGCGKAQNSTELAAEEYTLMSIDTIINGKEGVFPGLIPILNSY
LENMEVDVDTRCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEMNYSL
ILKCNQIANELCECPELLGSAFRKVKYSGSKTDSSN

• ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine

• GCS (PF03074 )

• None

• None

• Cytoplasmic

ATGGGGCTGCTGTCCCAGGGCTCGCCGCTGAGCTGGGAGGAAACCAAGCGCCATGCCGAC
CACGTGCGGCGGCACGGGATCCTCCAGTTCCTGCACATCTACCACGCCGTCAAGGACCGG
CACAAGGACGTTCTCAAGTGGGGCGATGAGGTGGAATACATGTTGGTATCTTTTGATCAT
GAAAATAAAAAAGTCCGGTTGGTCCTGTCTGGGGAGAAAGTTCTTGAAACTCTGCAAGAG
AAGGGGGAAAGGACAAACCCAAACCATCCTACCCTTTGGAGACCAGAGTATGGGAGTTAC
ATGATTGAAGGGACACCAGGACAGCCCTACGGAGGAACAATGTCCGAGTTCAATACAGTT
GAGGCCAACATGCGAAAACGCCGGAAGGAGGCTACTTCTATATTAGAAGAAAATCAGGCT
CTTTGCACAATAACTTCATTTCCCAGATTAGGCTGTCCTGGGTTCACACTGCCCGAGGTC
AAACCCAACCCAGTGGAAGGAGGAGCTTCCAAGTCCCTCTTCTTTCCAGATGAAGCAATA
AACAAGCACCCTCGCTTCAGTACCTTAACAAGAAATATCCGACATAGGAGAGGAGAAAAG
GTTGTCATCAATGTACCAATATTTAAGGACAAGAATACACCATCTCCATTTATAGAAACA
TTTACTGAGGATGATGAAGCTTCAAGGGCTTCTAAGCCGGATCATATTTACATGGATGCC
ATGGGATTTGGAATGGGCAATTGCTGTCTCCAGGTGACATTCCAAGCCTGCAGTATATCT
GAGGCCAGATACCTTTATGATCAGTTGGCTACTATCTGTCCAATTGTTATGGCTTTGAGT
GCTGCATCTCCCTTTTACCGAGGCTATGTGTCAGACATTGATTGTCGCTGGGGAGTGATT
TCTGCATCTGTAGATGATAGAACTCGGGAGGAGCGAGGACTGGAGCCATTGAAGAACAAT
AACTATAGGATCAGTAAATCCCGATATGACTCAATAGACAGCTATTTATCTAAGTGTGGT
GAGAAATATAATGACATCGACTTGACGATAGATAAAGAGATCTACGAACAGCTGTTGCAG
GAAGGCATTGATCATCTCCTGGCCCAGCATGTTGCTCATCTCTTTATTAGAGACCCACTG
ACACTGTTTGAAGAGAAAATACACCTGGATGATGCTAATGAGTCTGACCATTTTGAGAAT
ATTCAGTCCACAAATTGGCAGACAATGAGATTTAAGCCCCCTCCTCCAAACTCAGACATT
GGATGGAGAGTAGAATTTCGACCCATGGAGGTGCAATTAACAGACTTTGAGAACTCTGCC
TATGTGGTGTTTGTGGTACTGCTCACCAGAGTGATCCTTTCCTACAAATTGGATTTTCTC
ATTCCACTGTCAAAGGTTGATGAGAACATGAAGGTAGCACAGAAAAGAGATGCTGTCTTG
CAGGGAATGTTTTATTTCAGGAAAGATATTTGCAAAGGTGGCAATGCAGTGGTGGATGGT
TGTGGCAAGGCCCAGAACAGCACGGAGCTCGCTGCAGAGGAGTACACCCTCATGAGCATA
GACACCATCATCAATGGGAAGGAAGGTGTGTTTCCTGGACTGATCCCAATTCTGAACTCT
TACCTTGAAAACATGGAAGTGGATGTGGACACCAGATGTAGTATTCTGAACTACCTAAAG
CTAATTAAGAAGAGAGCATCTGGAGAACTAATGACAGTTGCCAGATGGATGAGGGAGTTT
ATCGCAAACCATCCTGACTACAAGCAAGACAGTGTCATAACTGATGAAATGAATTATAGC
CTTATTTTGAAGTGTAACCAAATTGCAAATGAATTATGTGAATGCCCAGAGTTACTTGGA
TCAGCATTTAGGAAAGTAAAATATAGTGGAAGTAAAACTGACTCATCCAACTAG

1. Beutler E, Gelbart T, Kondo T, Matsunaga AT: The molecular basis of a case of gamma-glutamylcysteine synthetase deficiency. Blood. 1999 Oct 15;94(8):2890-4. [PubMed ]
2. Ristoff E, Augustson C, Geissler J, de Rijk T, Carlsson K, Luo JL, Andersson K, Weening RS, van Zwieten R, Larsson A, Roos D: A missense mutation in the heavy subunit of gamma-glutamylcysteine synthetase gene causes hemolytic anemia. Blood. 2000 Apr 1;95(7):2193-6. [PubMed ]
3. Gipp JJ, Chang C, Mulcahy RT: Cloning and nucleotide sequence of a full-length cDNA for human liver gamma-glutamylcysteine synthetase. Biochem Biophys Res Commun. 1992 May 29;185(1):29-35. [PubMed ]
4. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
5. Mulcahy RT, Gipp JJ: Identification of a putative antioxidant response element in the 5'-flanking region of the human gamma-glutamylcysteine synthetase heavy subunit gene. Biochem Biophys Res Commun. 1995 Apr 6;209(1):227-33. [PubMed ]

1. Ashida H, Sawa Y, Shibata H: Cloning, biochemical and phylogenetic characterizations of gamma-glutamylcysteine synthetase from Anabaena sp. PCC 7120. Plant Cell Physiol. 2005 Apr;46(4):557-62. Epub 2005 Feb 2. [PubMed ]
2. Srivastava S, Chan C: Application of metabolic flux analysis to identify the mechanisms of free fatty acid toxicity to human hepatoma cell line. Biotechnol Bioeng. 2007 Jul 5;. [PubMed ]

1. EC 6.3.2.3
2. GSH synthetase
3. GSH-S
4. Glutathione synthase

MATNWGSLLQDKQQLEELARQAVDRALAEGVLLRTSQEPTSSEVVSYAPFTLFPSLVPSA
LLEQAYAVQMDFNLLVDAVSQNAAFLEQTLSSTIKQDDFTARLFDIHKQVLKEGIAQTVF
LGLNRSDYMFQRSADGSPALKQIEINTISASFGGLASRTPAVHRHVLSVLSKTKEAGKIL
SNNPSKGLALGIAKAWELYGSPNALVLLIAQEKERNIFDQRAIENELLARNIHVIRRTFE
DISEKGSLDQDRRLFVDGQEIAVVYFRDGYMPRQYSLQNWEARLLLERSHAAKCPDIATQ
LAGTKKVQQELSRPGMLEMLLPGQPEAVARLRATFAGLYSLDVGEEGDQAIAEALAAPSR
FVLKPQREGGGNNLYGEEMVQALKQLKDSEERASYILMEKIEPEPFENCLLRPGSPARVV
QCISELGIFGVYVRQEKTLVMNKHVGHLLRTKAIEHADGGVAAGVAVLDNPYPV

• ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione

• GSH_synthase (PF03199 )
• GSH_synth_ATP (PF03917 )

• None

• None

ATGGCCACCAACTGGGGGAGCCTCTTGCAGGATAAACAGCAGCTAGAGGAGCTGGCACGG
CAGGCCGTGGACCGGGCCCTGGCTGAGGGAGTATTGCTGAGGACCTCACAGGAGCCCACT
TCCTCGGAGGTGGTGAGCTATGCCCCATTCACGCTCTTCCCCTCACTGGTCCCCAGTGCC
CTGCTGGAGCAAGCCTATGCTGTGCAGATGGACTTCAACCTGCTAGTGGATGCTGTCAGC
CAGAACGCTGCCTTCCTGGAGCAAACTCTTTCCAGCACCATCAAACAGGATGACTTTACC
GCTCGTCTCTTTGACATCCACAAGCAAGTCCTAAAAGAGGGCATTGCCCAGACTGTGTTC
CTGGGCCTGAATCGCTCAGACTACATGTTCCAGCGCAGCGCAGATGGCTCCCCAGCCCTG
AAACAGATCGAAATCAACACCATCTCTGCCAGCTTTGGGGGCCTGGCCTCCCGGACCCCA
GCTGTGCACCGACATGTTCTCAGTGTCCTGAGTAAGACCAAAGAAGCTGGCAAGATCCTC
TCTAATAATCCCAGCAAGGGACTGGCCCTGGGAATTGCCAAAGCCTGGGAGCTCTACGGC
TCACCCAATGCTCTGGTGCTACTGATTGCTCAAGAGAAGGAAAGAAACATATTTGACCAG
CGTGCCATAGAGAATGAGCTACTGGCCAGGAACATCCATGTGATCCGACGAACATTTGAA
GATATCTCTGAAAAGGGGTCTCTGGACCAAGACCGAAGGCTGTTTGTGGATGGCCAGGAA
ATTGCTGTGGTTTACTTCCGGGATGGCTACATGCCTCGTCAGTACAGTCTACAGAATTGG
GAAGCACGTCTACTGCTGGAGAGGTCACATGCTGCCAAGTGCCCAGACATTGCCACCCAG
CTGGCTGGGACTAAGAAGGTGCAGCAGGAGCTAAGCAGGCCGGGCATGCTGGAGATGTTG
CTCCCTGGCCAGCCTGAGGCTGTGGCCCGCCTCCGCGCCACCTTTGCTGGCCTCTACTCA
CTGGATGTGGGTGAAGAAGGGGACCAGGCCATCGCCGAGGCCCTTGCTGCCCCTAGCCGG
TTTGTGCTAAAGCCCCAGAGAGAGGGTGGAGGTAACAACCTATATGGGGAGGAAATGGTA
CAGGCCCTGAAACAGCTGAAGGACAGTGAGGAGAGGGCCTCCTACATCCTCATGGAGAAG
ATCGAACCTGAGCCTTTTGAGAATTGCCTGCTACGGCCTGGCAGCCCTGCCCGAGTGGTC
CAGTGCATTTCAGAGCTGGGCATCTTTGGGGTCTATGTCAGGCAGGAAAAGACACTCGTG
ATGAACAAGCACGTGGGGCATCTACTTCGAACCAAAGCCATCGAGCATGCAGATGGTGGT
GTGGCAGCGGGAGTGGCAGTCCTGGACAACCCATACCCTGTGTGA

1. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed ]
2. Gali RR, Board PG: Sequencing and expression of a cDNA for human glutathione synthetase. Biochem J. 1995 Aug 15;310 ( Pt 1):353-8. [PubMed ]
3. Shi ZZ, Habib GM, Rhead WJ, Gahl WA, He X, Sazer S, Lieberman MW: Mutations in the glutathione synthetase gene cause 5-oxoprolinuria. Nat Genet. 1996 Nov;14(3):361-5. [PubMed ]
4. Dahl N, Pigg M, Ristoff E, Gali R, Carlsson B, Mannervik B, Larsson A, Board P: Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction. Hum Mol Genet. 1997 Jul;6(7):1147-52. [PubMed ]

1. Tanaka T, Halicka HD, Huang X, Traganos F, Darzynkiewicz Z: Constitutive histone H2AX phosphorylation and ATM activation, the reporters of DNA damage by endogenous oxidants. Cell Cycle. 2006 Sep;5(17):1940-5. Epub 2006 Sep 1. [PubMed ]

1. Beta- thionase
2. EC 4.2.1.22
3. Serine sulfhydrase

PSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPAS
ESPHHHTAPAKSPKILPDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKDR
ISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVL
RALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEIL
QQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTTY
EVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAA
QELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLSA
PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGK
VIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLLN
FVAAQERDQK

• L-serine + L-homocysteine = L-cystathionine + H2O

• PALP (PF00291 )
• CBS (PF00571 )

• None

• None

• Cytoplasm

ATGCCTTCTGAGACCCCCCAGGCAGAAGTGGGGCCCACAGGCTGCCCCCACCGCTCAGGG
CCACACTCGGCGAAGGGGAGCCTGGAGAAGGGGTCCCCAGAGGATAAGGAAGCCAAGGAG
CCCCTGTGGATCCGGCCCGATGCTCCGAGCAGGTGCACCTGGCAGCTGGGCCGGCCTGCC
TCCGAGTCCCCACATCACCACACTGCCCCGGCAAAATCTCCAAAAATCTTGCCAGATATT
CTGAAGAAAATCGGGGACACCCCTATGGTCAGAATCAACAAGATTGGGAAGAAGTTCGGC
CTGAAGTGTGAGCTCTTGGCCAAGTGTGAGTTCTTCAACGCGGGCGGGAGCGTGAAGGAC
CGCATCAGCCTGCGGATGATTGAGGATGCTGAGCGCGACGGGACGCTGAAGCCCGGGGAC
ACGATTATCGAGCCGACATCCGGGAACACCGGGATCGGGCTGGCCCTGGCTGCGGCAGTG
AGGGGCTATCGCTGCATCATCGTGATGCCAGAGAAGATGAGCTCCGAGAAGGTGGACGTG
CTGCGGGCACTGGGGGCTGAGATTGTGAGGACGCCCACCAATGCCAGGTTCGACTCCCCG
GAGTCACACGTGGGGGTGGCCTGGCGGCTGAAGAACGAAATCCCCAATTCTCACATCCTA
GACCAGTACCGCAACGCCAGCAACCCCCTGGCTCACTACGACACCACCGCTGATGAGATC
CTGCAGCAGTGTGATGGGAAGCTGGACATGCTGGTGGCTTCAGTGGGCACGGGCGGCACC
ATCACGGGCATTGCCAGGAAGCTGAAGGAGAAGTGTCCTGGATGCAGGATCATTGGGGTG
GATCCCGAAGGGTCCATCCTCGCAGAGCCGGAGGAGCTGAACCAGACGGAGCAGACAACC
TACGAGGTGGAAGGGATCGGCTACGACTTCATCCCCACGGTGCTGGACAGGACGGTGGTG
GACAAGTGGTTCAAGAGCAACGATGAGGAGGCGTTCACCTTTGCCCGCATGCTGATCGCG
CAAGAGGGGCTGCTGTGCGGTGGCAGTGCTGGCAGCACGGTGGCGGTGGCCGTGAAGGCT
GCGCAGGAGCTGCAGGAGGGCCAGCGCTGCGTGGTCATTCTGCCCGACTCAGTGCGGAAC
TACATGACCAAGTTCCTGAGCGACAGGTGGATGCTGCAGAAGGGCTTTCTGAAGGAGGAG
GACCTCACGGAGAAGAAGCCCTGGTGGTGGCACCTCCGTGTTCAGGAGCTGGGCCTGTCA
GCCCCGCTGACCGTGCTCCCGACCATCACCTGTGGGCACACCATCGAGATCCTCCGGGAG
AAGGGCTTCGACCAGGCGCCCGTGGTGGATGAGGCGGGGGTAATCCTGGGAATGGTGACG
CTTGGGAACATGCTCTCGTCCCTGCTTGCCGGGAAGGTGCAGCCGTCAGACCAAGTTGGC
AAAGTCATCTACAAGCAGTTCAAACAGATCCGCCTCACGGACACGCTGGGCAGGCTCTCG
CACATCCTGGAGATGGACCACTTCGCCCTGGTGGTGCACGAGCAGATCCAGTACCACAGC
ACCGGGAAGTCCAGTCAGCGGCAGATGGTGTTCGGGGTGGTCACCGCCATTGACTTGCTG
AACTTCGTGGCCGCCCAGGAGCGGGACCAGAAGTGA

1. Kraus JP, Janosik M, Kozich V, Mandell R, Shih V, Sperandeo MP, Sebastio G, de Franchis R, Andria G, Kluijtmans LA, Blom H, Boers GH, Gordon RB, Kamoun P, Tsai MY, Kruger WD, Koch HG, Ohura T, Gaustadnes M: Cystathionine beta-synthase mutations in homocystinuria. Hum Mutat. 1999;13(5):362-75. [PubMed ]
2. de Franchis R, Kraus E, Kozich V, Sebastio G, Kraus JP: Four novel mutations in the cystathionine beta-synthase gene: effect of a second linked mutation on the severity of the homocystinuric phenotype. Hum Mutat. 1999;13(6):453-7. [PubMed ]
3. Meier M, Janosik M, Kery V, Kraus JP, Burkhard P: Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein. EMBO J. 2001 Aug 1;20(15):3910-6. [PubMed ]
4. Taoka S, Lepore BW, Kabil O, Ojha S, Ringe D, Banerjee R: Human cystathionine beta-synthase is a heme sensor protein. Evidence that the redox sensor is heme and not the vicinal cysteines in the CXXC motif seen in the crystal structure of the truncated enzyme. Biochemistry. 2002 Aug 20;41(33):10454-61. [PubMed ]
5. Kozich V, Kraus JP: Screening for mutations by expressing patient cDNA segments in E. coli: homocystinuria due to cystathionine beta-synthase deficiency. Hum Mutat. 1992;1(2):113-23. [PubMed ]
6. Kraus J, Packman S, Fowler B, Rosenberg LE: Purification and properties of cystathionine beta-synthase from human liver. Evidence for identical subunits. J Biol Chem. 1978 Sep 25;253(18):6523-8. [PubMed ]
7. Hu FL, Gu Z, Kozich V, Kraus JP, Ramesh V, Shih VE: Molecular basis of cystathionine beta-synthase deficiency in pyridoxine responsive and nonresponsive homocystinuria. Hum Mol Genet. 1993 Nov;2(11):1857-60. [PubMed ]
8. Sperandeo MP, Panico M, Pepe A, Candito M, de Franchis R, Kraus JP, Andria G, Sebastio G: Molecular analysis of patients affected by homocystinuria due to cystathionine beta-synthase deficiency: report of a new mutation in exon 8 and a deletion in intron 11. J Inherit Metab Dis. 1995;18(2):211-4. [PubMed ]
9. Chasse JF, Paly E, Paris D, Paul V, Sinet PM, Kamoun P, London J: Genomic organization of the human cystathionine beta-synthase gene: evidence for various cDNAs. Biochem Biophys Res Commun. 1995 Jun 26;211(3):826-32. [PubMed ]
10. Shih VE, Fringer JM, Mandell R, Kraus JP, Berry GT, Heidenreich RA, Korson MS, Levy HL, Ramesh V: A missense mutation (I278T) in the cystathionine beta-synthase gene prevalent in pyridoxine-responsive homocystinuria and associated with mild clinical phenotype. Am J Hum Genet. 1995 Jul;57(1):34-9. [PubMed ]
11. 7635485 Kluijtmans LA, Blom HJ, Boers GH, van Oost BA, Trijbels FJ, van den Heuvel LP: Two novel missense mutations in the cystathionine beta-synthase gene in homocystinuric patients. Hum Genet. 1995 Aug;96(2):249-50.
12. 7762555 Sebastio G, Sperandeo MP, Panico M, de Franchis R, Kraus JP, Andria G: The molecular basis of homocystinuria due to cystathionine beta-synthase deficiency in Italian families, and report of four novel mutations. Am J Hum Genet. 1995 Jun;56(6):1324-33.
13. 7849717 Marble M, Geraghty MT, de Franchis R, Kraus JP, Valle D: Characterization of a cystathionine beta-synthase allele with three mutations in cis in a patient with B6 nonresponsive homocystinuria. Hum Mol Genet. 1994 Oct;3(10):1883-6.
14. 7903580 Kraus JP, Le K, Swaroop M, Ohura T, Tahara T, Rosenberg LE, Roper MD, Kozich V: Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells. Hum Mol Genet. 1993 Oct;2(10):1633-8.
15. 7967489 Kraus JP: Komrower Lecture. Molecular basis of phenotype expression in homocystinuria. J Inherit Metab Dis. 1994;17(4):383-90.
16. 7981678 de Franchis R, Kozich V, McInnes RR, Kraus JP: Identical genotypes in siblings with different homocystinuric phenotypes: identification of three mutations in cystathionine beta-synthase using an improved bacterial expression system. Hum Mol Genet. 1994 Jul;3(7):1103-8.
17. 8022826 Kruger WD, Cox DR: A yeast system for expression of human cystathionine beta-synthase: structural and functional conservation of the human and yeast genes. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6614-8.
18. 8353501 Kozich V, de Franchis R, Kraus JP: Molecular defect in a patient with pyridoxine-responsive homocystinuria. Hum Mol Genet. 1993 Jun;2(6):815-6.
19. 8528202 Kruger WD, Cox DR: A yeast assay for functional detection of mutations in the human cystathionine beta-synthase gene. Hum Mol Genet. 1995 Jul;4(7):1155-61.
20. 8755636 Kluijtmans LA, Boers GH, Stevens EM, Renier WO, Kraus JP, Trijbels FJ, van den Heuvel LP, Blom HJ: Defective cystathionine beta-synthase regulation by S-adenosylmethionine in a partially pyridoxine responsive homocystinuria patient. J Clin Invest. 1996 Jul 15;98(2):285-9.
21. 8803779 Sperandeo MP, Candito M, Sebastio G, Rolland MO, Turc-Carel C, Giudicelli H, Dellamonica P, Andria G: Homocysteine response to methionine challenge in four obligate heterozygotes for homocystinuria and relationship with cystathionine beta-synthase mutations. J Inherit Metab Dis. 1996;19(3):351-6.
22. 8990018 Aral B, Coude M, London J, Aupetit J, Chasse JF, Zabot MT, Chadefaux-Vekemans B, Kamoun P: Two novel mutations (K384E and L539S) in the C-terminal moiety of the cystathionine beta-synthase protein in two French pyridoxine-responsive homocystinuria patients. Hum Mutat. 1997;9(1):81-2.
23. 9156316 Dawson PA, Cox AJ, Emmerson BT, Dudman NP, Kraus JP, Gordon RB: Characterisation of five missense mutations in the cystathionine beta-synthase gene from three patients with B6-nonresponsive homocystinuria. Eur J Hum Genet. 1997 Jan-Feb;5(1):15-21.
24. 9266356 Kozich V, Janosik M, Sokolova J, Oliveriusova J, Orendac M, Kraus JP, Elleder D: Analysis of CBS alleles in Czech and Slovak patients with homocystinuria: report on three novel mutations E176K, W409X and 1223 + 37 del99. J Inherit Metab Dis. 1997 Jul;20(3):363-6.
25. 9361025 Kim CE, Gallagher PM, Guttormsen AB, Refsum H, Ueland PM, Ose L, Folling I, Whitehead AS, Tsai MY, Kruger WD: Functional modeling of vitamin responsiveness in yeast: a common pyridoxine-responsive cystathionine beta-synthase mutation in homocystinuria. Hum Mol Genet. 1997 Dec;6(13):2213-21.
26. 9383285 Chasse JF, Paul V, Escanez R, Kamoun P, London J: Human cystathionine beta-synthase: gene organization and expression of different 5' alternative splicing. Mamm Genome. 1997 Dec;8(12):917-21.
27. 9790750 Kraus JP, Oliveriusova J, Sokolova J, Kraus E, Vlcek C, de Franchis R, Maclean KN, Bao L, Bukovsk, Patterson D, Paces V, Ansorge W, Kozich V: The human cystathionine beta-synthase (CBS) gene: complete sequence, alternative splicing, and polymorphisms. Genomics. 1998 Sep 15;52(3):312-24.

1. Bhatia M, Wong FL, Fu D, Lau HY, Moochhala SM, Moore PK: Role of hydrogen sulfide in acute pancreatitis and associated lung injury. FASEB J. 2005 Apr;19(6):623-5. Epub 2005 Jan 25. [PubMed ]
2. Zhang H, Zhi L, Moore PK, Bhatia M: Role of hydrogen sulfide in cecal ligation and puncture-induced sepsis in the mouse. Am J Physiol Lung Cell Mol Physiol. 2006 Jun;290(6):L1193-201. Epub 2006 Jan 20. [PubMed ]
3. Oh GS, Pae HO, Lee BS, Kim BN, Kim JM, Kim HR, Jeon SB, Jeon WK, Chae HJ, Chung HT: Hydrogen sulfide inhibits nitric oxide production and nuclear factor-kappaB via heme oxygenase-1 expression in RAW264.7 macrophages stimulated with lipopolysaccharide. Free Radic Biol Med. 2006 Jul 1;41(1):106-19. Epub 2006 Apr 25. [PubMed ]
4. Lowicka E, Beltowski J: Hydrogen sulfide (H2S) - the third gas of interest for pharmacologists. Pharmacol Rep. 2007 Jan-Feb;59(1):4-24. [PubMed ]
5. Tamizhselvi R, Moore PK, Bhatia M: Hydrogen sulfide acts as a mediator of inflammation in acute pancreatitis: in vitro studies using isolated mouse pancreatic acinar cells. J Cell Mol Med. 2007 Mar-Apr;11(2):315-26. [PubMed ]

1. EC 2.6.1.1
2. Glutamate oxaloacetate transaminase 1
3. Transaminase A

APPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQKI
ANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFLA
RWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLENA
PEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWAI
RYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPPA
QGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGMF
SFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ

• L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate

• Aminotran_1_2 (PF00155 )

• None

• None

• Cytoplasm

ATGGCACCTCCGTCAGTCTTTGCCGAGGTTCCGCAGGCCCAGCCTGTCCTGGTCTTCAAG
CTCACTGCCGACTTCAGGGAGGATCCGGACCCCCGCAAGGTCAACCTGGGAGTGGGAGCA
TATCGCACGGATGACTGCCATCCCTGGGTTTTGCCAGTAGTGAAGAAAGTGGAGCAGAAG
ATTGCTAATGACAATAGCCTAAATCACGAGTATCTGCCAATCCTGGGCCTGGCTGAGTTC
CGGAGCTGTGCTTCTCGTCTTGCCCTTGGGGATGACAGCCCAGCACTCAAGGAGAAGCGG
GTAGGAGGTGTGCAATCTTTGGGGGGAACAGGTGCACTTCGAATTGGAGCTGATTTCTTA
GCGCGTTGGTACAATGGAACAAACAACAAGAACACACCTGTCTATGTGTCCTCACCAACC
TGGGAGAATCACAATGCTGTGTTTTCCGCTGCTGGTTTTAAAGACATTCGGTCCTATCGC
TACTGGGATGCAGAGAAGAGAGGATTGGACCTCCAGGGCTTCCTGAATGATCTGGAGAAT
GCTCCTGAGTTCTCCATTGTTGTCCTCCACGCCTGTGCACACAACCCAACTGGGATTGAC
CCAACTCCGGAGCAGTGGAAGCAGATTGCTTCTGTCATGAAGCACCGGTTTCTGTTCCCC
TTCTTTGACTCAGCCTATCAGGGCTTCGCATCTGGAAACCTGGAGAGAGATGCCTGGGCC
ATTCGCTATTTTGTGTCTGAAGGCTTCGAGTTCTTCTGTGCCCAGTCCTTCTCCAAGAAC
TTCGGGCTCTACAATGAGAGAGTCGGGAATCTGACTGTGGTTGGAAAAGAACCTGAGAGC
ATCCTGCAAGTCCTTTCCCAGATGGAGAAGATCGTGCGGATTACTTGGTCCAATCCCCCC
GCCCAGGGAGCACGAATTGTGGCCAGCACCCTCTCTAACCCTGAGCTCTTTGAGGAATGG
ACAGGTAATGTGAAGACAATGGCTGACCGGATTCTGACCATGAGATCTGAACTCAGGGCA
CGACTAGAAGCCCTCAAAACCCCTGGGACCTGGAACCACATCACTGATCAAATTGGCATG
TTCAGCTTCACTGGGTTGAACCCCAAGCAGGTTGAGTATCTGGTCAATGAAAAGCACATC
TACCTGCTGCCAAGTGGTCGAATCAACGTGAGTGGCTTAACCACCAAAAATCTAGATTAC
GTGGCCACCTCCATCCATGAAGCAGTCACCAAAATCCAGTGA

1. Bousquet-Lemercier B, Pol S, Pave-Preux M, Hanoune J, Barouki R: Properties of human liver cytosolic aspartate aminotransferase mRNAs generated by alternative polyadenylation site selection. Biochemistry. 1990 Jun 5;29(22):5293-9. [PubMed ]
2. Doyle JM, Schinina ME, Bossa F, Doonan S: The amino acid sequence of cytosolic aspartate aminotransferase from human liver. Biochem J. 1990 Sep 15;270(3):651-7. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. CDO
2. CDO-I
3. Cysteine dioxygenase type I
4. EC 1.13.11.20

MEQTEVLKPRTLADLIRILHQLFAGDEVNVEEVQAIMEAYESDPTEWAMYAKFDQYRYTR
NLVDQGNGKFNLMILCWGEGHGSSIHDHTNSHCFLKMLQGNLKETLFAWPDKKSNEMVKK
SERVLRENQCAYINDSIGLHRVENISHTEPAVSLHLYSPPFDTCHAFDQRTGHKNKVTMT
FHSKFGIRTPNATSGSLENN

• L-cysteine + O2 = 3-sulfinoalanine

• CDO_I (PF05995 )

• None

• None

ATGGAACAGACCGAAGTGCTGAAGCCACGGACCCTGGCTGATCTGATCCGCATCCTGCAC
CAGCTCTTTGCCGGCGATGAGGTCAATGTAGAGGAGGTGCAGGCCATCATGGAAGCCTAC
GAGAGCGACCCCATCGAGTGGGCAATGTACGCCAAGTTCGACCAGTACAGGTATACCCGA
AATCTTGTGGATCAAGGAAATGGAAAATTTAATCTGATGATTCTCTGTTGGGGTGAAGGA
CATGGCAGCAGTATTCATGATCATACCAACTCCCACTGCTTTCTGAAGATGCTACAGGGA
AATCTAAAGGAGACATTATTTGCCTGGCCTGACAAAAAATCCAATGAGATGGTCAAGAAG
TCTGAAAGAGTCTTGAGGGAAAACCAGTGTGCCTACATCAATGATTCCATTGGCTTACAT
CGAGTAGAGAACATCAGCCATACGGAACCTGCTGTGAGCCTTCACTTGTACAGTCCACCT
TTTGATACATGCCATGCCTTTGATCAAAGAACAGGACATAAAAACAAAGTCACAATGACA
TTCCATAGTAAATTTGGAATCAGAACTCCAAATGCAACTTCGGGCTCGCTGGAGAACAAC
TAA

1. McCann KP, Akbari MT, Williams AC, Ramsden DB: Human cysteine dioxygenase type I: primary structure derived from base sequencing of cDNA. Biochim Biophys Acta. 1994 Nov 16;1209(1):107-10. [PubMed ]
2. Ramsden DB, Kapadi A, Fitch NJ, Farmer MJ, Bennett P, Williams AC: Human cysteine dioxygenase type I (CDO-I; EC 1.13.11.20): 5' flanking region and intron-exon structure of the gene. Mol Pathol. 1997 Oct;50(5):269-71. [PubMed ]

1. Roopnarinesingh ES, Steventon GB, Harris RM, Waring RH, Mitchell SC: Induction of cysteine dioxygenase activity by oral administration of cysteine analogues to the rat: implications for drug efficacy and safety. Drug Metabol Drug Interact. 2005;21(2):75-86. [PubMed ]
2. McCoy JG, Bailey LJ, Bitto E, Bingman CA, Aceti DJ, Fox BG, Phillips GN Jr: Structure and mechanism of mouse cysteine dioxygenase. Proc Natl Acad Sci U S A. 2006 Feb 28;103(9):3084-9. Epub 2006 Feb 21. [PubMed ]
3. Ye S, Wu X, Wei L, Tang D, Sun P, Bartlam M, Rao Z: An insight into the mechanism of human cysteine dioxygenase. Key roles of the thioether-bonded tyrosine-cysteine cofactor. J Biol Chem. 2007 Feb 2;282(5):3391-402. Epub 2006 Nov 29. [PubMed ]
4. Jin HF, DU SX, Zhao X, Zhang SQ, Tian Y, Bu DF, Tang CS, DU JB: [Significance of endogenous sulfur dioxide in the regulation of cardiovascular system] Beijing Da Xue Xue Bao. 2007 Aug 18;39(4):423-5. [PubMed ]

1. EC 6.3.2.2
2. GCS light chain
3. Gamma- glutamylcysteine synthetase
4. Gamma-ECS
5. Glutamate--cysteine ligase modifier subunit

MGTDSRAAKALLARARTLHLQTGNLLNWGRLRKKCPSTHSEELHDCIQKTLNEWSSQINP
DLVREFPDVLECTVSHAVEKINPDEREEMKVSAKLFIVESNSSSSTRSAVDMACSVLGVA
QLDSVIIASPPIEDGVNLSLEHLQPYWEELENLVQSKKIVAIGTSDLDKTQLEQLYQWAQ
VKPNSNQVNLASCCVMPPDLTAFAKQFDIQLLTHNDPKELLSEASFQEALQESIPDIQAH
EWVPLWLLRYSVIVKSRGIIKSKGYILQAKRRGS

• ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine

• None

• None

ATGGGCACCGACAGCCGCGCGGCCAAGGCGCTCCTGGCGCGGGCCCGCACCCTGCACCTG
CAGACGGGGAACCTGCTGAACTGGGGCCGCCTGCGGAAGAAGTGCCCGTCCACGCACAGC
GAGGAGCTTCATGATTGTATCCAAAAAACCTTGAATGAATGGAGTTCCCAAATCAACCCA
GATTTGGTCAGGGAGTTTCCAGATGTCTTGGAATGCACTGTATCTCATGCAGTAGAAAAG
ATAAATCCTGATGAAAGAGAAGAAATGAAAGTTTCTGCAAAACTGTTCATTGTAGAATCA
AACTCTTCATCATCAACTAGAAGTGCAGTTGACATGGCCTGTTCAGTCCTTGGAGTTGCA
CAGCTGGATTCTGTGATCATTGCTTCACCTCCTATTGAAGATGGAGTTAATCTTTCCTTG
GAGCATTTACAGCCTTACTGGGAGGAATTAGAAAACTTAGTTCAGAGCAAAAAGATTGTT
GCCATAGGTACCTCTGATCTAGACAAAACACAGTTGGAACAGCTGTATCAGTGGGCACAG
GTAAAACCAAATAGTAACCAAGTTAATCTTGCCTCCTGCTGTGTGATGCCACCAGATTTG
ACTGCATTTGCTAAACAATTTGACATACAGCTGTTGACTCACAATGATCCAAAAGAACTG
CTTTCTGAAGCAAGTTTCCAAGAAGCTCTTCAGGAAAGCATTCCTGACATTCAAGCGCAC
GAGTGGGTGCCGCTGTGGCTACTGCGGTATTCGGTCATTGTGAAAAGTAGAGGAATTATC
AAATCAAAAGGCTACATTTTACAAGCTAAAAGAAGGGGTTCTTAA

1. Gipp JJ, Bailey HH, Mulcahy RT: Cloning and sequencing of the cDNA for the light subunit of human liver gamma-glutamylcysteine synthetase and relative mRNA levels for heavy and light subunits in human normal tissues. Biochem Biophys Res Commun. 1995 Jan 17;206(2):584-9. [PubMed ]

1. Ashida H, Sawa Y, Shibata H: Cloning, biochemical and phylogenetic characterizations of gamma-glutamylcysteine synthetase from Anabaena sp. PCC 7120. Plant Cell Physiol. 2005 Apr;46(4):557-62. Epub 2005 Feb 2. [PubMed ]

1. CysRS
2. Cysteine--tRNA ligase
3. EC 6.1.1.16

MADSSGQQGKGRRVQPQWSPPAGTQPCRLHLYNSLTRNKEVFIPQDGKKVTWYCCGPTVY
DASHMGHARSYISFDILRRVLKDYFKFDVFYCMNITDIDDKIIKRARQNHLFEQYREKRP
EAAQLLEDVQAALKPFSVKLNETTDPDKKQMLERIQHAVQLATEPLEKAVQSRLTGEEVN
SCVEVLLEEAKDLLSDWLDSTLGCDVTDNSIFSKLPKFWEGDFHRDMEALNVLPPDVLTR
VSEYVPEIVNFVQKIVDNGYGYVSNGSVYFDTAKFASSEKHSYGKLVPEAVGDQKALQEG
EGDLSISADRLSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASM
DIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDA
LKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFLNEFFLNVKDILRAPVDITGQF
EKWGEEEAELNKNFYDKKTAIHKALCDNVDTRTVMEEMRALVSQCNLYMAARKAVRKRPN
QALLENIALYLTHMLKIFGAVEEDSSLGFPVGGPGTSLSLEATVMPYLQVLSEFREGVRK
IAREQKVPEILQLSDALRDNILPELGVRFEDHEGLPTVVKLVDRNTLLKEREEKRRVEEE
KRKKKEEAARRKQEQEAAKLAKMKIPPSEMFLSETDKYSKFDENGLPTHDMEGKELSKGQ
AKKLKKLFEAQEKLYKEYLQMAQNGSFQ

• ATP + L-cysteine + tRNACys = AMP + diphosphate + L-cysteinyl-tRNACys

• tRNA-synt_1e (PF01406 )

• None

• None

• Cytoplasm

ATGGCAGATTCCTCCGGGCAGCAGGGCAAAGGCCGGCGTGTGCAGCCCCAGTGGTCCCCT
CCTGCTGGGACCCAGCCATGCAGACTCCACCTTTACAACAGCCTCACCAGGAACAAGGAA
GTGTTCATACCTCAAGATGGGAAAAAGGTGACGTGGTATTGCTGTGGGCCAACCGTCTAT
GACGCATCTCACATGGGGCACGCCAGGTCCTACATCTCTTTTGATATCTTGAGAAGAGTG
TTGAAGGATTACTTCAAATTTGATGTCTTTTATTGCATGAACATTACGGATATTGATGAC
AAGATCATCAAGAGGGCCCGGCAGAACCACCTGTTCGAGCAGTATCGGGAGAAGAGGCCT
GAAGCGGCACAGCTCTTGGAGGATGTTCAGGCCGCCCTGAAGCCATTTTCAGTAAAATTA
AATGAGACCACGGATCCCGATAAAAAGCAGATGCTCGAACGGATTCAGCACGCAGTGCAG
CTTGCCACAGAGCCACTTGAGAAAGCTGTGCAGTCCAGACTCACGGGAGAGGAAGTCAAC
AGCTGTGTGGAGGTGTTGCTGGAAGAAGCCAAGGATTTGCTCTCTGACTGGCTGGATTCT
ACACTTGGCTGTGATGTCACTGACAATTCCATCTTCTCCAAGCTGCCCAAGTTCTGGGAG
GGGGACTTCCACAGAGACATGGAAGCTCTGAATGTTCTCCCTCCAGATGTCTTAACCCGG
GTTAGTGAGTATGTGCCAGAAATTGTGAACTTTGTCCAGAAGATTGTGGACAACGGTTAC
GGCTATGTCTCCAATGGGTCTGTCTACTTTGATACAGCGAAGTTTGCTTCTAGCGAGAAG
CACTCCTATGGGAAGCTGGTGCCTGAGGCCGTTGGAGATCAGAAAGCCCTTCAAGAAGGG
GAAGGTGACCTGAGCATCTCTGCAGACCGCCTGAGTGAGAAGCGCTCTCCCAACGACTTT
GCCTTATGGAAGGCCTCTAAGCCCGGAGAACCGTCCTGGCCGTGCCCTTGGGGAAAGGGT
CGTCCGGGCTGGCATATCGAGTGCTCGGCCATGGCAGGCACCCTCCTAGGGGCTTCGATG
GACATTCACGGAGGTGGGTTCGACCTCCGGTTCCCCCACCATGACAATGAGCTGGCACAG
TCGGAGGCCTACTTTGAAAACGACTGCTGGGTCAGGTACTTCCTGCACACAGGCCACCTG
ACCATTGCAGGCTGCAAAATGTCAAAGTCACTAAAAAACTTCATCACCATTAAAGATGCC
TTGAAAAAGCACTCAGCACGGCAGTTGCGGCTGGCCTTCCTCATGCACTCGTGGAAGGAC
ACCCTGGACTACTCCAGCAACACCATGGAGTCAGCGCTTCAATATGAGAAGTTCTTGAAT
GAGTTTTTCTTAAATGTGAAAGATATCCTTCGCGCTCCTGTTGACATCACTGGTCAGTTT
GAGAAGTGGGGAGAAGAAGAAGCAGAACTGAATAAGAACTTTTATGACAAGAAGACAGCA
ATTCACAAAGCCCTCTGTGACAATGTTGACACCCGCACCGTCATGGAAGAGATGCGGGCC
TTGGTCAGTCAGTGCAACCTCTATATGGCAGCCCGGAAAGCCGTGAGGAAGAGGCCCAAC
CAGGCTCTGCTGGAGAACATCGCCCTGTACCTCACCCATATGCTGAAGATCTTTGGGGCC
GTAGAAGAGGACAGCTCCCTGGGATTCCCGGTCGGAGGGCCTGGAACCAGCCTCAGTCTC
GAGGCCACAGTCATGCCCTACCTTCAGGTGTTATCAGAATTCCGAGAAGGAGTGCGGAAG
ATTGCCCGAGAGCAAAAAGTCCCTGAGATTCTGCAGCTCAGCGATGCCCTGCGGGACAAC
ATCCTGCCCGAGCTTGGGGTGCGGTTTGAAGACCACGAAGGACTGCCCACAGTGGTGAAA
CTGGTAGACAGAAACACCTTATTAAAAGAGAGAGAAGAAAAGAGACGGGTTGAAGAGGAG
AAGAGGAAGAAGAAAGAGGAGGCGGCCCGGAGGAAACAGGAACAAGAAGCAGCAAAGCTG
GCCAAGATGAAGATTCCCCCCAGTGAGATGTTCTTGTCAGAAACCGACAAATACTCCAAG
TTTGATGAAAATGGTCTGCCCACACATGACATGGAGGGCAAAGAGCTCAGCAAAGGGCAA
GCCAAGAAGCTGAAGAAGCTCTTCGAGGCTCAGGAGAAGCTCTACAAGGAATATCTGCAG
ATGGCCCAGAATGGAAGCTTCCAGTGA

1. Davidson E, Caffarella J, Vitseva O, Hou YM, King MP: Isolation of two cDNAs encoding functional human cytoplasmic cysteinyl-tRNA synthetase. Biol Chem. 2001 Mar;382(3):399-406. [PubMed ]
2. Cools J, Wlodarska I, Somers R, Mentens N, Pedeutour F, Maes B, De Wolf-Peeters C, Pauwels P, Hagemeijer A, Marynen P: Identification of novel fusion partners of ALK, the anaplastic lymphoma kinase, in anaplastic large-cell lymphoma and inflammatory myofibroblastic tumor. Genes Chromosomes Cancer. 2002 Aug;34(4):354-62. [PubMed ]
3. Cruzen ME, Arfin SM: Nucleotide and deduced amino acid sequence of human cysteinyl-tRNA synthetase. DNA Seq. 1994;4(4):243-8. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. EC 4.4.1.1
2. Gamma-cystathionase

MQEKDASSQGFLPHFQHFATQAIHVGQDPEQWTSRAVVPPISLSTTFKQGAPGQHSGFEY
SRSGNPTRNCLEKAVAALDGAKYCLAFASGLAATVTITHLLKAGDQIICMDDVYGGTNRY
FRQVASEFGLKISFVDCSKIKLLEAAITPETKLVWIETPTNPTQKVIDIEGCAHIVHKHG
DIILVVDNTFMSPYFQRPLALGADISMYSATKYMNGHSDVVMGLVSVNCESLHNRLRFLQ
NSLGAVPSPIDCYLCNRGLKTLHVRMEKHFKNGMAVAQFLESNPWVEKVIYPGLPSHPQH
ELVKRQCTGCTGMVTFYIKGTLQHAEIFLKNLKLFTLAESLGGFESLAELPAIMTHASVL
KNDRDVLGISDTLIRLSVGLEDEEDLLEDLDQALKAAHPPSGSHS

• L-cystathionine + H2O = L-cysteine + NH3 + 2-oxobutanoate

• Cys_Met_Meta_PP (PF01053 )

• None

• None

• Cytoplasm

ATGCAGGAAAAAGACGCCTCCTCACAAGGTTTCCTGCCACACTTCCAACATTTCGCCACG
CAGGCGATCCATGTGGGCCAGGATCCGGAGCAATGGACCTCCAGGGCTGTAGTGCCCCCC
ATCTCACTGTCCACCACGTTCAAGCAAGGGGCGCCTGGCCAGCACTCGGGTTTTGAATAT
AGCCGTTCTGGAAATCCCACTAGGAATTGCCTTGAAAAAGCAGTGGCAGCACTGGATGGG
GCTAAGTACTGTTTGGCCTTTGCTTCAGGTTTAGCAGCCACTGTAACTATTACCCATCTT
TTAAAAGCAGGAGACCAAATTATTTGTATGGATGATGTGTATGGAGGTACAAACAGGTAC
TTCAGGCAAGTGGCATCTGAATTTGGATTAAAGATTTCTTTTGTTGATTGTTCCAAAATC
AAATTACTAGAGGCAGCAATTACACCAGAAACCAAGCTTGTTTGGATCGAAACCCCCACA
AACCCCACCCAGAAGGTGATTGACATTGAAGGCTGTGCACATATTGTCCATAAGCATGGA
GACATTATTTTGGTCGTGGATAACACTTTTATGTCACCATATTTCCAGCGCCCTTTGGCT
CTGGGAGCTGATATTTCTATGTATTCTGCAACAAAATACATGAATGGCCACAGTGATGTT
GTAATGGGCCTGGTGTCTGTTAATTGTGAAAGCCTTCATAATAGACTTCGTTTCTTGCAA
AACTCTCTTGGAGCAGTTCCATCTCCTATTGATTGTTACCTCTGCAATCGAGGTCTGAAG
ACTCTACATGTCCGAATGGAAAAGCATTTCAAAAACGGAATGGCAGTTGCCCAGTTCCTG
GAATCTAATCCTTGGGTAGAAAAGGTTATTTATCCTGGGCTGCCCTCTCATCCACAGCAT
GAGTTGGTGAAGCGTCAGTGTACAGGTTGTACAGGGATGGTCACCTTTTATATTAAGGGC
ACTCTTCAGCATGCTGAGATTTTCCTCAAGAACCTAAAGCTATTTACTCTGGCCGAGAGC
TTGGGAGGATTCGAAAGCCTTGCTGAGCTTCCGGCAATCATGACTCATGCATCAGTTCTT
AAGAATGACAGAGATGTCCTTGGAATTAGTGACACACTGATTCGACTTTCTGTGGGCTTA
GAGGATGAGGAAGACCTACTGGAAGATCTAGATCAAGCTTTGAAGGCAGCACACCCTCCA
AGTGGAATTCACAGCTAG

1. Wang J, Hegele RA: Genomic basis of cystathioninuria (MIM 219500) revealed by multiple mutations in cystathionine gamma-lyase (CTH). Hum Genet. 2003 Apr;112(4):404-8. Epub 2003 Feb 6. [PubMed ]
2. Lu Y, O'Dowd BF, Orrego H, Israel Y: Cloning and nucleotide sequence of human liver cDNA encoding for cystathionine gamma-lyase. Biochem Biophys Res Commun. 1992 Dec 15;189(2):749-58. [PubMed ]

1. Fiorucci S, Antonelli E, Mencarelli A, Orlandi S, Renga B, Rizzo G, Distrutti E, Shah V, Morelli A: The third gas: H2S regulates perfusion pressure in both the isolated and perfused normal rat liver and in cirrhosis. Hepatology. 2005 Sep;42(3):539-48. [PubMed ]
2. Zhang H, Zhi L, Moore PK, Bhatia M: Role of hydrogen sulfide in cecal ligation and puncture-induced sepsis in the mouse. Am J Physiol Lung Cell Mol Physiol. 2006 Jun;290(6):L1193-201. Epub 2006 Jan 20. [PubMed ]
3. Wallace JL, Dicay M, McKnight W, Martin GR: Hydrogen sulfide enhances ulcer healing in rats. FASEB J. 2007 Jul 18;. [PubMed ]

1. Solute carrier family 19 member 3
2. ThTr-2
3. ThTr2

MDCYRTSLSSSWIYPTVILCLFGFFSMMRPSEPFLIPYLSGPDKNLTSAEITNEIFPVWT
YSYLVLLLPVFVLTDYVRYKPVIILQGISFIITWLLLLFGQGVKTMQVVEFFYGMVTAAE
VAYYAYIYSVVSPEHYQRVSGYCRSVTLAAYTAGSVLAQLLVSLANMSYFYLNVISLASV
SVAFLFSLFLPMPKKSMFFHAKPSREIKKSSSVNPVLEETHEGEAPGCEEQKPTSEILST
SGKLNKGQLNSLKPSNVTVDVFVQWFQDLKECYSSKRLFYWSLWWAFATAGFNQVLNYVQ
ILWDYKAPSQDSSIYNGAVEAIATFGGAVAAFAVGYVKVNWDLLGELALVVFSVVNAGSL
FLMHYTANIWACYAGYLIFKSSYMLLITIAVFQIAVNLNVERYALVFGINTFIALVIQTI
MTVIVVDQRGLNLPVSIQFLVYGSYFAVIAGIFLMRSMYITYSTKSQKDVQSPAPSENPD
VSHPEEESNIIMSTKL

• Folate_carrier (PF01770 )

• None

• 8-28
• 54-74
• 82-102
• 111-131
• 145-165
• 170-190
• 283-303
• 317-337
• 343-363
• 376-396
• 406-426
• 435-455

• Membrane
• multi-pass membrane protein (Potential)

ATGGATTGTTACAGAACTTCACTAAGCAGTTCCTGGATTTACCCCACTGTGATCCTCTGC
TTATTTGGTTTTTTCTCCATGATGAGACCCTCAGAACCATTCCTTATCCCATATTTATCT
GGACCAGATAAAAACCTGACCAGTGCAGAGATAACAAATGAGATCTTCCCCGTTTGGACA
TACTCCTACCTGGTGCTGCTGCTGCCTGTGTTTGTCCTCACCGATTATGTCCGCTACAAG
CCAGTCATCATCTTGCAAGGTATCAGTTTCATCATTACCTGGCTGCTGCTGTTGTTTGGC
CAAGGAGTGAAGACCATGCAGGTTGTAGAGTTCTTCTATGGGATGGTCACCGCCGCCGAG
GTGGCCTACTACGCCTACATATACAGCGTGGTCAGCCCCGAGCACTACCAGAGAGTGAGC
GGCTACTGCAGGAGCGTCACGCTGGCCGCCTACACAGCAGGGTCGGTGCTGGCTCAACTC
TTGGTATCCCTGGCGAACATGTCGTACTTTTACCTCAACGTCATATCCTTGGCCTCTGTC
TCCGTGGCTTTCCTTTTCTCACTTTTCCTACCAATGCCCAAGAAAAGCATGTTTTTTCAT
GCAAAACCCAGCAGAGAAATAAAGAAGTCATCAAGCGTGAATCCAGTATTAGAGGAAACT
CACGAAGGTGAAGCACCAGGCTGTGAAGAGCAGAAACCCACATCAGAAATACTCAGCACT
TCAGGGAAGCTGAATAAGGGCCAGCTGAACAGCCTGAAACCAAGCAATGTGACTGTGGAC
GTTTTTGTGCAGTGGTTCCAAGATTTGAAGGAGTGCTACTCCTCAAAACGTCTTTTCTAC
TGGTCTCTATGGTGGGCTTTCGCCACAGCAGGTTTTAACCAGGTTTTGAACTATGTTCAA
ATCCTGTGGGATTACAAGGCGCCATCCCAAGATTCTTCCATCTATAATGGGGCCGTAGAA
GCTATTGCAACCTTTGGAGGGGCTGTGGCTGCCTTTGCAGTGGGTTATGTGAAAGTCAAC
TGGGACCTTCTGGGAGAGCTGGCTCTGGTGGTCTTCTCAGTTGTCAATGCCGGTTCTTTA
TTTCTCATGCATTACACAGCCAATATCTGGGCGTGCTATGCTGGCTATTTGATATTCAAG
TCCAGCTATATGCTTCTTATAACCATAGCAGTATTTCAGATTGCAGTTAATCTGAATGTG
GAACGCTATGCCTTGGTATTTGGAATCAACACCTTTATTGCCTTGGTGATTCAGACCATC
ATGACTGTGATTGTAGTAGATCAGAGAGGGCTCAACTTGCCAGTCAGCATTCAGTTTTTA
GTTTATGGGAGCTATTTTGCAGTAATTGCTGGAATTTTCCTAATGAGAAGCATGTATATT
ACCTACTCAACCAAATCCCAGAAGGATGTACAGAGCCCTGCTCCAAGTGAGAATCCAGAT
GTGTCTCACCCAGAGGAAGAGAGTAATATCATCATGTCAACAAAACTCTAA

1. Eudy JD, Spiegelstein O, Barber RC, Wlodarczyk BJ, Talbot J, Finnell RH: Identification and characterization of the human and mouse SLC19A3 gene: a novel member of the reduced folate family of micronutrient transporter genes. Mol Genet Metab. 2000 Dec;71(4):581-90. [PubMed ]

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]

1. 6-O- methylguanine-DNA methyltransferase
2. EC 2.1.1.63
3. MGMT
4. O-6-methylguanine-DNA- alkyltransferase

MDKDCEMKRTTLDSPLGKLELSGCEQGLHEIKLLGKGTSAADAVEVPAPAAVLGGPEPLM
QCTAWLNAYFHQPEAIEEFPVPALHHPVFQQESFTRQVLWKLLKVVKFGEVISYQQLAAL
AGNPKAARAVGGAMRGNPVPILIPCHRVVCSSGAVGNYSGGLAVKEWLLAHEGHRLGKPG
LGGSSGLAGAWLKGAGATSGSPPAGRN

• DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine

• DNA_binding_1 (PF01035 )
• Methyltransf_1N (PF02870 )

• None

• None

• Nucleus

ATGGACAAGGATTGTGAAATGAAACGCACCACACTGGACAGCCCTTTGGGGAAGCTGGAG
CTGTCTGGTTGTGAGCAGGGTCTGCACGAAATAAAGCTCCTGGGCAAGGGGACGTCTGCA
GCTGATGCCGTGGAGGTCCCAGCCCCCGCTGCGGTTCTCGGAGGTCCGGAGCCCCTGATG
CAGTGCACAGCCTGGCTGAATGCCTATTTCCACCAGCCCGAGGCTATCGAAGAGTTCCCC
GTGCCGGCACTTCACCATCCCGTTTTCCAGCAAGAGTCGTTCACCAGACAGGTGTTATGG
AAGCTGCTGAAGGTTGTGAAATTCGGAGAAGTGATTTCTTACCAGCAATTAGCAGCCCTG
GCAGGCAACCCCAAAGCCGCGCGAGCAGTGGGAGGAGCAATGAGAGGCAATCCTGTCCCC
ATCCTCATCCCGTGCCACAGAGTGGTCTGCAGCAGCGGAGCCGTGGGCAACTACTCCGGA
GGACTGGCCGTGAAGGAATGGCTTCTGGCCCATGAAGGCCACCGGTTGGGGAAGCCAGGC
TTGGGAGGGAGCTCAGGTCTGGCAGGGGCCTGGCTCAAGGGAGCGGGAGCTACCTCGGGC
TCCCCGCCTGCTGGCCGAAACTGA

1. von Wronski MA, Shiota S, Tano K, Mitra S, Bigner DD, Brent TP: Structural and immunological comparison of indigenous human O6-methylguanine-DNA methyltransferase with that encoded by a cloned cDNA. J Biol Chem. 1991 Jan 15;266(2):1064-70. [PubMed ]
2. Rydberg B, Spurr N, Karran P: cDNA cloning and chromosomal assignment of the human O6-methylguanine-DNA methyltransferase. cDNA expression in Escherichia coli and gene expression in human cells. J Biol Chem. 1990 Jun 5;265(16):9563-9. [PubMed ]
3. Hayakawa H, Koike G, Sekiguchi M: Expression and cloning of complementary DNA for a human enzyme that repairs O6-methylguanine in DNA. J Mol Biol. 1990 Jun 20;213(4):739-47. [PubMed ]
4. Koike G, Maki H, Takeya H, Hayakawa H, Sekiguchi M: Purification, structure, and biochemical properties of human O6-methylguanine-DNA methyltransferase. J Biol Chem. 1990 Sep 5;265(25):14754-62. [PubMed ]
5. Tano K, Shiota S, Collier J, Foote RS, Mitra S: Isolation and structural characterization of a cDNA clone encoding the human DNA repair protein for O6-alkylguanine. Proc Natl Acad Sci U S A. 1990 Jan;87(2):686-90. [PubMed ]
6. Liem LK, Lim A, Li BF: Specificities of human, rat and E. coli O6-methylguanine-DNA methyltransferases towards the repair of O6-methyl and O6-ethylguanine in DNA. Nucleic Acids Res. 1994 May 11;22(9):1613-9. [PubMed ]

1. Niture SK, Velu CS, Smith QR, Bhat GJ, Srivenugopal KS: Increased expression of the MGMT repair protein mediated by cysteine prodrugs and chemopreventative natural products in human lymphocytes and tumor cell lines. Carcinogenesis. 2007 Feb;28(2):378-89. Epub 2006 Aug 31. [PubMed ]

1. CysRS
2. Cysteine--tRNA ligase
3. EC 6.1.1.16
4. Probable cysteinyl-tRNA synthetase, mitochondrial precursor

MLRTTRGPGLGPPLLQAALGLGRAGWHWPAGRAASGGRGRAWLQPTGRETGVQVYNSLTG
RKEPLIVAHAEAASWYSCGPTVYDHAHLGHACSYVRFDIIRRILTKVFGCSIVMVMGITD
VDDKIIKRANEMNISPASLASLYEEDFKQDMAALKVLPPTVYLRVTENIPQIISFIEGII
ARGNAYSTAKGNVYFDLKSRGDKYGKLVGVVPGPVGEPADSDKRHASDFALWKAAKPQEV
FWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAFPHHENEIAQCEVFHQCEQWG
NYFLHSGHLHAKGKEEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYSDSAM
LQAQQLLLGLGSFLEDARAYMKGQLACGSVREAMLWERLSSTKRAVKAALADDFDTPRVV
DAILGLAHHGNGQLRASLKEPEGPRSPAVFGAIISYFEQFFETVGISLANQQYVSGDGSE
ATLHGVVDELVRFRQKVRQFALAMPEATGDARRQQLLERQPLLEACDTLRRGLTAHGINI
KDRSSTTSTWELLDQRTKDQKSAG

• ATP + L-cysteine + tRNACys = AMP + diphosphate + L-cysteinyl-tRNACys

• tRNA-synt_1e (PF01406 )

• None

• None

• Mitochondrion

ATGTTGAGGACTACGCGCGGCCCAGGCCTGGGCCCCCCGCTGCTCCAGGCCGCGCTGGGC
CTTGGGCGGGCTGGGTGGCACTGGCCTGCGGGCCGGGCGGCGAGCGGGGGGCGCGGGCGG
GCCTGGCTGCAGCCCACGGGCCGGGAGACGGGTGTGCAGGTGTACAACAGCCTCACCGGG
AGGAAGGAACCCCTAATCGTGGCGCACGCCGAAGCCGCCTCCTGGTATAGCTGTGGACCA
ACTGTATATGATCATGCGCACCTTGGCCATGCTTGCTCATATGTTAGATTTGATATCATT
CGAAGGATCCTAACCAAGGTTTTTGGATGCAGCATAGTCATGGTGATGGGTATTACAGAT
GTAGATGATAAAATCATCAAAAGAGCCAATGAGATGAATATTTCCCCCGCTTCCCTCGCC
AGTCTTTATGAGGAAGACTTCAAGCAGGACATGGCAGCCCTGAAGGTTCTCCCACCCACG
GTGTACCTGAGGGTAACCGAAAATATTCCTCAGATAATTTCTTTCATTGAAGGAATCATT
GCTCGTGGGAACGCTTATTCAACGGCAAAAGGCAATGTCTACTTCGATCTGAAGTCTAGA
GGAGACAAGTATGGCAAATTGGTCGGCGTGGTCCCTGGTCCAGTCGGAGAGCCAGCGGAC
TCTGACAAGCGTCATGCCAGTGACTTCGCCCTGTGGAAGGCGGCCAAACCCCAGGAGGTG
TTCTGGGCCTCTCCCTGGGGACCCGGGAGGCCGGGCTGGCACATCGAGTGCTCTGCCATC
GCTAGTATGGTATTTGGAAGTCAACTGGATATCCATTCAGGTGGGATAGATTTAGCTTTT
CCACATCATGAGAACGAAATTGCACAGTGCGAAGTCTTTCATCAGTGCGAGCAGTGGGGA
AATTATTTTCTGCATTCTGGGCATTTGCACGCCAAAGGCAAAGAAGAAAAAATGTCCAAA
TCATTAAAGAACTACATTACTATTAAGGACTTTCTGAAGACCTTTTCCCCCGATGTCTTC
CGGTTCTTCTGCCTGCGGAGCAGCTACCGCTCAGCCATCGACTACAGTGACAGCGCCATG
CTCCAAGCTCAGCAGCTGCTCCTGGGGCTGGGCTCTTTCCTGGAGGACGCACGTGCCTAC
ATGAAGGGGCAGCTGGCCTGCGGCTCCGTCAGGGAAGCGATGCTGTGGGAGAGGCTCTCC
AGCACCAAGAGGGCCGTGAAGGCGGCCTTGGCAGATGATTTTGACACACCCAGGGTGGTT
GATGCCATCCTGGGCCTTGCACACCACGGGAATGGACAGCTCAGGGCGTCCCTGAAGGAA
CCTGAAGGGCCGAGAAGTCCTGCTGTGTTTGGTGCCATCATCTCTTACTTTGAACAGTTT
TTTGAAACTGTTGGAATTTCTCTGGCAAATCAACAGTACGTTTCAGGAGACGGCAGCGAG
GCTACCTTGCATGGTGTGGTGGACGAGCTGGTGCGGTTCCGGCAGAAGGTCCGGCAGTTT
GCGCTGGCCATGCCCGAGGCCACGGGGGACGCCCGGCGGCAGCAGCTCCTAGAAAGGCAG
CCCCTGCTGGAAGCATGCGACACCCTGCGCCGGGGCCTGACTGCCCACGGCATCAACATC
AAGGACAGAAGCAGTACAACATCCACGTGGGAACTGCTGGATCAAAGGACAAAAGACCAA
AAATCAGCGGGCTGA

1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed ]
2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed ]