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Showing drug card for Pyrazinamide (DB00339)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-04-16 16:47:38
Primary Accession Number DB00339
Secondary Accession Number
  • APRD01206
Name Pyrazinamide
Drug Type
  • Approved
  • Small Molecule
Description A pyrazine that is used therapeutically as an antitubercular agent. [PubChem]
Synonyms
  1. PZA
  2. Pirazimida
  3. Pirazinamid
  4. Pyrazinamdie
  5. Pyrazine carboxylamide
  6. Pyrazineamide
  7. Pyrazinecarboxamide
  8. Pyrazinecarboxylic acid amide
  9. Pyrazinoic acid amide
Brand Names
  1. Aldinamid
  2. Aldinamide
  3. Braccopiral
  4. Corsazinmid
  5. Dipimide
  6. Eprazin
  7. Farmizina
  8. Isopas
  9. Lynamide
  10. Novamid
  11. Pezetamid
  12. Piraldina
  13. Pirilene
  14. Prazina
  15. Pyrafat
  16. Pyramide
  17. Pyrazide
  18. Pyrazinamide BP 2000
  19. Rifater
  20. Rozide
  21. Tebrazid
  22. Tebrazio
  23. Unipyranamide
  24. Zinamide
  25. Zinastat
  26. pms-Pyrazinamide
Brand Mixtures
  1. Rifater - Tab (Isoniazid + Pyrazinamide + Rifampin)
Chemical IUPAC Name pyrazine-2-carboxamide
Chemical Formula C5H5N3O
Chemical Structure Structure
CAS Registry Number 98-96-4
InChI Identifier InChI=1/C5H5N3O/c6-5(9)4-3-7-1-2-8-4/h1-3H,(H2,6,9)/f/h6H2
InChI Key IPEHBUMCGVEMRF-MDVJYLRGCE
KEGG Drug D00144 Link Image
KEGG Compound C01956 Link Image
PubChem Compound 1046 Link Image
PubChem Substance 5057 Link Image
ChEBI ID 8656 Link Image
PharmGKB ID PA451182 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 00618810 Link Image
RxList Link http://www.rxlist.com/cgi/generic2/pyrazinamide.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Pyrazinamide Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 123.1127
Monoisotopic Molecular Weight 123.0433
State Solid
Melting Point 192 oC
Experimental Water Solubility 1.5E+004 mg/L Source: PhysProp
Predicted Water Solubility 9.37e+01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -1 Source: PhysProp
Predicted LogP -0.70 Calculated using ALOGPS
Experimental LogS -0.91 [ADME Research, USCD]
Predicted LogS -0.12 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point -0.5
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Isomeric SMILES NC(=O)C1=NC=CN=C1
Canonical SMILES NC(=O)C1=NC=CN=C1
Drug Category
  • Antitubercular Agents
ATC Codes
AHFS Codes
  • 08:16.04
Indication For the initial treatment of active tuberculosis in adults and children when combined with other antituberculous agents.
Pharmacology Pyrazinamide kills or stops the growth of certain bacteria that cause tuberculosis (TB). It is used with other drugs to treat tuberculosis. It is a highly specific agent and is active only against Mycobacterium tuberculosis. In vitro and in vivo, the drug is active only at a slightly acid pH.
Mechanism of Action Pyrazinamide is an important sterilizing drug that shortens tuberculosis (TB) therapy. However, the mechanism of action of pyrazinamide is poorly understood because of its unusual properties. In literature it has been written that the pyrazinoic acid (POA), the active moiety of pyrazinamide, disrupted membrane energetics and inhibited membrane transport function at acid pH in Mycobacterium tuberculosis. The antimycobacterial activity appears to partly depend on conversion of the drug to POA. Susceptible strains of M. tuberculosis produce pyrazinamidase, an enzyme that deaminates pyrazinamide to POA, and the vitro susceptibility of a given strain of the organism appears to correspond to its pyrazinamidase activity. Experimental evidence suggests that pyrazinamide diffuses into M. tuberculosis in a passive manner, is converted into POA by pyrazinamidase, and because of an inefficient efflux system, accumulates in huge amounts in the bacterial cytoplasm. The accumulation of POA lowers the intracellular pH to a suboptimal level that is likely to inactivate a vital target enzyme such as fatty acid synthase.
Absorption Rapidly and well absorbed from the gastrointestinal tract.
Toxicity Side effects include liver injury, arthralgias, anorexia, nausea and vomiting, dysuria,malaise and fever, sideroblastic anemia, adverse effects on the blood clotting mechanism or vascular integrity, and hypersensitivity reactions such as urticaria, pruritis and skin rashes.
Protein Binding ~10% (bound to plasma proteins)
Biotransformation Hepatic.
Half Life 9-10 hours (normal conditions)
Dosage Forms
Form Route
Tablet Oral
Patient Information Not Available
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Cyclosporine Pyrazinamide decreases the effect of cyclosporine
Food Interactions
  • Take without regard to meals.
Pathways Not Available
General References
  1. Yee D, Valiquette C, Pelletier M, Parisien I, Rocher I, Menzies D: Incidence of serious side effects from first-line antituberculosis drugs among patients treated for active tuberculosis. Am J Respir Crit Care Med. 2003 Jun 1;167(11):1472-7. Epub 2003 Jan 31. [PubMed Link Image]
  2. : Controlled trial of four thrice-weekly regimens and a daily regimen all given for 6 months for pulmonary tuberculosis. Lancet. 1981 Jan 24;1(8213):171-4. [PubMed Link Image]
  3. : Controlled clinical trial of 4 short-couse regimens of chemotherapy (three 6-month and one 8-month) for pulmonary tuberculosis. Tubercle. 1983 Sep;64(3):153-66. [PubMed Link Image]
  4. : A controlled trial of 6 months' chemotherapy in pulmonary tuberculosis. Final report: results during the 36 months after the end of chemotherapy and beyond. British Thoracic Society. Br J Dis Chest. 1984 Oct;78(4):330-6. [PubMed Link Image]
  5. Drugs.com Link Image
  6. Wikipedia Link Image
  7. RxList Link Image
Organisms Affected
  • Mycobacterium tuberculosis
Phase 1 Metabolizing Enzymes
  1. Xanthine dehydrogenase/oxidase
Targets
  1. Cyclopropane-fatty-acyl-phospholipid synthase 1
  2. Fatty acid synthase
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Xanthine dehydrogenase/oxidase
Enzyme 1 Gene Name XDH
Enzyme 1 SwissProt ID P47989 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P47989|XDH_HUMAN Xanthine dehydrogenase/oxidase 
TADKLVFFVNGRKVVEKNADPETTLLAYLRRKLGLSGTKLGCGEGGCGACTVMLSKYDRL
QNKIVHFSANACLAPICSLHHVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGIV
MSMYTLLRNQPEPTMEEIENAFQGNLCRCTGYRPILQGFRTFARDGGCCGGDGNNPNCCM
NQKKDHSVSLSPSLFKPEEFTPLDPTQEPIFPPELLRLKDTPRKQLRFEGERVTWIQAST
LKELLDLKAQHPDAKLVVGNTEIGIEMKFKNMLFPMIVCPAWIPELNSVEHGPDGISFGA
ACPLSIVEKTLVDAVAKLPAQKTEVFRGVLEQLRWFAGKQVKSVASVGGNIITASPISDL
NPVFMASGAKLTLVSRGTRRTVQMDHTFFPGYRKTLLSPEEILLSIEIPYSREGEYFSAF
KQASRREDDIAKVTSGMRVLFKPGTTEVQELALCYGGMANRTISALKTTQRQLSKLWKEE
LLQDVCAGLAEELHLPPDAPGGMVDFRCTLTLSFFFKFYLTVLQKLGQENLEDKCGKLDP
TFASATLLFQKDPPADVQLFQEVPKGQSEEDMVGRPLPHLAADMQASGEAVYCDDIPRYE
NELSLRLVTSTRAHAKIKSIDTSEAKKVPGFVCFISADDVPGSNITGICNDETVFAKDKV
TCVGHIIGAVVADTPEHTQRAAQGVKITYEELPAIITIEDAIKNNSFYGPELKIEKGDLK
KGFSEADNVVSGEIYIGGQEHFYLETHCTIAVPKGEAGEMELFVSTQNTMKTQSFVAKML
GVPANRIVVRVKRMGGGFGGKETRSTVVSTAVALAAYKTGRPVRCMLDRDEDMLITGGRH
PFLARYKVGFMKTGTVVALEVDHFSNVGNTQDLSQSIMERALFHMDNCYKIPNIRGTGRL
CKTNLPSNTAFRGFGGPQGMLIAECWMSEVAVTCGMPAEEVRRKNLYKEGDLTHFNQKLE
GFTLPRCWEECLASSQYHARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGAL
LHVYTDGSVLLTHGGTEMGQGLHTKMVQVASRALKIPTSKIYISETSTNTVPNTSPTAAS
VSADLNGQAVYAACQTILKRLEPYKKKNPSGSWEDWVTAAYMDTVSLSATGFYRTPNLGY
SFETNSGNPFHYFSYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAFV
QGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPIEFRVSLLRDCPNKKAIYASKAVG
EPPLFLAASIFFAIKDAIRAARAQHTGNNVKELFRLDSPATPEKIRNACVDKFTTLCVTG
VPENCKPWSVRV
Drug Target 1 [top]
Target 1 ID 181
Target 1 Name Cyclopropane-fatty-acyl-phospholipid synthase 1
Target 1 Synonyms
  1. CFA synthase
  2. Cyclopropane fatty acid synthase
  3. Cyclopropane mycolic acid synthase 1
  4. EC 2.1.1.79
Target 1 Gene Name cmaA1
Target 1 Protein Sequence >Cyclopropane-fatty-acyl-phospholipid synthase 1 
MPDELKPHFANVQAHYDLSDDFFRLFLDPTQTYSCAYFERDDMTLQEAQIAKIDLALGKL
GLQPGMTLLDVGCGWGATMMRAVEKYDVNVVGLTLSKNQANHVQQLVANSENLRSKRVLL
AGWEQFDEPVDRIVSIGAFEHFGHERYDAFFSLAHRLLPADGVMLLHTITGLHPKEIHER
GLPMSFTFARFLKFIVTEIFPGGRLPSIPMVQECASANGFTVTRVQSLQPHYAKTLDLWS
AALQANKGQAIALQSEEVYERYMKYLTGCAEMFRIGYIDVNQFTCQK
Target 1 Number of Residues 291
Target 1 Molecular Weight 32462
Target 1 Theoretical pI 6.17
Target 1 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
S-adenosylmethionine-dependent methyltransferase activity
cyclopropane-fatty-acyl-phospholipid synthase activity
Process
physiological process
metabolism
biosynthesis
lipid biosynthesis
Component
Not Available
Target 1 General Function Cell wall/membrane/envelope biogenesis
Target 1 Specific Function Transfers a methylene group from S-adenosyl-L-methionine to the cis double bond of an unsaturated fatty acid chain resulting in the replacement of the double bond with a methylene bridge. Mycolic acids, which represent the major constituent of mycobacterial cell wall complex, act as substrates
Target 1 Pathways Not Available
Target 1 Reactions
  • S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Essential
Target 1 GenBank ID Protein 886102 Link Image
Target 1 UniProtKB/Swiss-Prot ID Q11195 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name CFA1_MYCTU Link Image
Target 1 PDB ID 1KPH Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Cytoplasm
Target 1 Gene Sequence >864 bp 
ATGCCCGACGAGCTGAAGCCGCACTTCGCCAACGTGCAGGCGCACTACGACCTGTCCGAC
GACTTCTTCCGGCTGTTCCTCGATCCCACTCAGACCTACAGCTGCGCCTACTTCGAGCGC
GACGACATGACGCTGCAAGAGGCGCAGATCGCCAAGATCGATCTCGCGCTGGGCAAACTC
GGATTGCAGCCGGGCATGACACTGTTGGACGTCGGCTGCGGCTGGGGCGCCACCATGATG
CGCGCGGTGGAAAAATACGACGTCAACGTCGTCGGTCTGACCCTGAGCAAAAACCAGGCC
AACCACGTTCAGCAGCTGGTCGCCAACTCCGAAAATCTACGCTCCAAACGCGTTCTGCTG
GCCGGCTGGGAACAGTTTGACGAGCCCGTCGACCGCATCGTCAGCATCGGTGCTTTCGAA
CATTTCGGTCACGAGCGCTACGACGCGTTCTTCAGCCTGGCGCATCGCCTGCTGCCCGCT
GACGGGGTCATGCTGCTGCACACCATCACCGGGTTGCATCCGAAAGAGATCCACGAACGC
GGCCTGCCCATGTCGTTCACCTTCGCTCGTTTCCTGAAATTCATTGTGACCGAGATCTTT
CCGGGTGGGCGGCTGCCCTCGATACCGATGGTGCAGGAGTGTGCCAGCGCAAACGGCTTC
ACCGTCACCAGAGTTCAATCGTTGCAGCCGCACTATGCGAAAACCCTCGACCTCTGGTCC
GCGGCGTTGCAGGCCAACAAGGGCCAGGCCATCGCGCTGCAATCCGAGGAAGTCTACGAG
CGGTATATGAAGTACCTCACCGGCTGCGCCGAGATGTTTCGCATCGGATACATCGACGTC
AACCAGTTCACCTGCCAGAAGTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID Not Available
Target 1 GenAtlas ID Not Available
Target 1 HGNC ID Not Available
Target 1 Chromosome Location Not Available
Target 1 Locus Not Available
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Fleischmann RD, Alland D, Eisen JA, Carpenter L, White O, Peterson J, DeBoy R, Dodson R, Gwinn M, Haft D, Hickey E, Kolonay JF, Nelson WC, Umayam LA, Ermolaeva M, Salzberg SL, Delcher A, Utterback T, Weidman J, Khouri H, Gill J, Mikula A, Bishai W, Jacobs Jr WR Jr, Venter JC, Fraser CM: Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains. J Bacteriol. 2002 Oct;184(19):5479-90. [PubMed Link Image]
  2. Yuan Y, Lee RE, Besra GS, Belisle JT, Barry CE 3rd: Identification of a gene involved in the biosynthesis of cyclopropanated mycolic acids in Mycobacterium tuberculosis. Proc Natl Acad Sci U S A. 1995 Jul 3;92(14):6630-4. [PubMed Link Image]
  3. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [PubMed Link Image]
Target 1 Drug References
  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 Link Image]
  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 Link Image]
Drug Target 2 [top]
Target 2 ID 1295
Target 2 Name Fatty acid synthase
Target 2 Synonyms
  1. EC 2.3.1.85
Target 2 Gene Name FASN
Target 2 Protein Sequence >Fatty acid synthase 
MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRWKAGLYGLPRRSGKLKDLSRF
DASFFGVHPKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEAL
SRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQC
PAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLAR
RVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVG
DPQELNGITRALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFH
SPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNVHIILRPNTQPPPAPAPHATL
PRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGP
EVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSILRSDEAVKPFGLKVSQLLLS
TDESTFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAV
LAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVTISGPQAPVFE
FVEQLRKEGVFAKEVRTGGMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEA
QWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLEIAPHALLQAVLKRGLKPSCT
IIPLMKKDHRDNLEFFLAGIGRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSL
AWDVPAAEDFPNGSGSPSAAIYNIDTSSESPDHYLVDHTLDGRVLFPATGYLSIVWKTLA
RALGLGVEQLPVVFEDVVLHQATILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQ
WDDPDPRLFDHPESPTPNPTEPLFLAQAEVYKELRLRGYDYGPHFQGILEASLEGDSGRL
LWKDNWVSFMDTMLQMSILGSAKHGLYLPTRVTAIHIDPATHRQKLYTLQDKAQVADVVV
SRWLRVTVAGGVHISGLHTESAPRRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQL
CKGLVQALQTTVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQ
VLAQERPKLPEDPLLSGLLDSPALKACLDTAVENMPSLKMKVVEVLAGHGHLYSRIPGLL
SPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSADLLVCNCAVA
ALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVAFLTSTEPQYGQGILSQDAWESL
FSRVSLRLVGLKKSFYGSTLFLCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSSRP
VWLKAINCATSGVVGLVNCLRREPGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKVLQGD
LVMNVYRDGAWGAFRHFLLEEDKPEEPTAHAFVSTLTRGDLSSIRWVCSSLRHAQPTCPG
AQLCTVYYASLNFRDIMLATGKLSPDAIPGKWTSQDSLLGMEFSGRDASGKRVMGLVPAK
GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGV
GQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSRDTSFEQHVLWHTGGKG
VDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFF
NESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQVLAEE
PEAVLKGAKPKLMSAISKTFCPAHKSYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGI
RTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLL
ENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSA
MERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLN
QPHMVLSSFVLAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSV
EVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELACPTPKEDGLAQQQTQLNLR
SLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLD
SIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGS
PTYVLAYTQSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAA
VDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGA
DYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEPRVSVREG
Target 2 Number of Residues 2552
Target 2 Molecular Weight 273403
Target 2 Theoretical pI 6.39
Target 2 GO Classification
Function
hydrolase activity
hydrolase activity, acting on ester bonds
oxidoreductase activity
vitamin binding
phosphopantetheine binding
binding
cofactor binding
catalytic activity
transferase activity
Process
biosynthesis
cellular metabolism
organic acid metabolism
carboxylic acid metabolism
fatty acid metabolism
fatty acid biosynthesis
physiological process
metabolism
Component
Not Available
Target 2 General Function Secondary metabolites biosynthesis, transport and catabolism
Target 2 Specific Function Fatty acid synthetase catalyzes the formation of long- chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein
Target 2 Pathways
Name SMPDB Link KEGG Link
Fatty acid biosynthesis (path 1) map00061 Link Image
Target 2 Reactions
  • (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH + H+
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 1049053 Link Image
Target 2 UniProtKB/Swiss-Prot ID P49327 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name FAS_HUMAN Link Image
Target 2 PDB ID 1XKT Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Cytoplasm. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to
Target 2 Gene Sequence >7515 bp 
ATGGAGGAGGTGGTGATTGCCGGCATGTTCGGGAAGCTGCCAGAGTCGGAGAACTTGCAG
GAGTTCTGGGACAACCTCATCGGCGGTGTGGACATGGTCACGGACGATGACCGTCGCTGG
AAGGCTGGGCTCTACGGCCTGCCCCGGCGGTCCGGCAAGCTGAAGGACCTGTCTAGGTTT
GATGCCTCCTTCTTCGGAGTCCACCCCAAGCAGGCACACACGATGGACCCTCAGCTGCGG
CTGCTGCTGGAAGCTACCTATGAAGCCATCGTGGACGGAGGCATCAACCCAGATTCACTC
CGAGGAACACACACTGGCGTCTGGGTGGGCGTGAGCGGCTCTGAGACCTCGGAGGCCCTG
AGCCGAGACCCCGAGACACTCGTGGGCTACAGCATGGTGGGCTGCCAGCGAGCGATGATG
GCCAACCGGCTCTCCTTCTTCTTCGACTTCAGAGGGCCCAGCATCGCACTGGACACAGCC
TGCTCCTCCAGCCTGATGGCCCTGCAGAACGCCTACCAGGCCATCCACAGCGGGCAGTGC
CCTGCCGCCATCGTGGGGGGCATCAACGTCCTGCTGAAGCCCAACACCTCCGTGCAGTTC
TTGAGGCTGGGGATGCTCAGCCCCGAGGGCACCTGCAAGGCCTTCGACACAGCGGGGAAT
GGGTACTGCCGCTCGGAGGGTGTGGTGGCTGTCCTGCTGACCAAGAAGTCCCTGGCCCGG
AAGGTCTACACCACCATCCTGAACAAAGGCACCAATACAGATGGCTTCAAGGAGCAAGGC
GTGACCTTCCCTCAGGATATCCAGGAGCAGCCTATCCGCTCGTTGTACCAGTCGGCCGGA
GTGGCCCCTGAGTCATTTGAATACATCGAAGCCCACGGACCAGGCACCAAGGTGGGCGAC
CCCCAGGAGCGTAATGGCATCACCCGAGCCCTGTGCGCCACCCGCCAGGAGCCGCTGCTC
ATCGGCTCCACCAAGTCCAACATGGGGCACCCGGAGCCAGCCTCGGGGCTCGACGCCCTG
GCCAAGGTGCTGCTGTCCCTGGAGCACGGGCTCTGGGCCCCCAACCTGCACTTCCATAGC
CCCAACCCTGAGATCCCAGCGCTGTTGGATGGGCGGCTGCAGGTGGTGGACCAGCCCCTG
CCCGTCCGTGGCGGCAACGTGGGCATCAACTCCTTTGGCTTCGGGGGCTCCAACATGCAC
ATCATCCTGAGGCCCAACACGCAGTCCGCCCCCGCACCCGCCCCACATGCCACCCTGCCC
CGTCTGCTGCGGGCCAGCGGACGCACCCCTGAGGCCGTGCAGAAGCTGCTGGAGCAGGGC
CTCCGGCACAGCCAGGGCCTGGCTTTCCTGAGCATGCTGAACGACATCGCGGCTGTCCCC
GCCACCGCCATGCCCTTCCGTGGCTACGCTGTGCTGGGTGGTGAGACGCGGTGGCCCAGA
GTGCAGCAGGTGCCCGCTGGCGAGCGCCCGCTCTGGTTCATCTGCTCTGGGATGGGCACA
CAGTGGCGTGGAATGGGGCTGAGCCTTATGCGCCTGGACCGCTTCCGAGATTCCATCCTA
CGCTCCGATGAGGCTGTGAACCGATTCGGCCTGAAGGTGTCACAGCTGCTGCTGAGCACA
GACGAGAGCACCTTTGATGACATCGTCCATTCGTTTGTGAGCCTGACTGCCATCCAGATA
GGCCTCATAGACCTGCTGAGCTGCATGGGACCTGAGGCAGATGGCATCGTCGGCCACTCC
CTGGGGGAGTGGCTGTCGGTACGCGACGGCTGCCTGTCCCAGGAGGAGGCCGTCCTCGCT
GCCTACTGGAGGGGACAGTGCATCAAAGAAGCCCCACTTCCCGCCGGCGCCATGGCAGCC
GTGGGCTTGTCCTGGGAGGAGTGTAAACAGCGCTGCCCCCCTGCGGTGGTGCCCGCCTGC
CACAACTCCAAGGACACAGTCACCATCTCGGGACCTCAGGCCCCGGTGTTTGAGTTCGTG
GAGCAGCTGAGGAAGGAGGGTGTGTTTGCCAAGGAGGTGCGGACCGGCGGTATGGCCTTC
CACTCCTACTTCATGGAGGCCATCGCACCCCCACTGCTGCAGGAGCTCAAGAAGGTGATC
CGGGAGCCGAAGCCACGTTCAGCCCGCTGGCTCAGCACCTCTATCCCCGAGGCCCAGTGG
CACAGCAGCCTGGCACGCACGTCTTCCGCCGAGTACAATGTCAACAACCTGGTGAGCCCT
GTGCTGTTCCAGGAGGCCCTGTGGCACGTGCCTGAGCACGCGGTGGTGCTGGAGATCGCC
CCGACCCCGTGCCCTCAGGCTGTCCTGAAGCGGGTCCGTAAGCCGAGCTGCACCATCATC
CCCCGTATGAAGAAGGATCACAGGGACAACCTGGAGTTCTTCCTGGCCGGCATCGGCAGG
CTGCACCTCTCAGGCATCGACGCCAACCCCAATGCCTTGTTCCCACCTGTGGAGTCCCCA
GCTCCCCGAGGAACTCCCCTCATCTCCCCACTCATCAAGTGGGACCACAGCCTGGCCTGG
GACGCGCCGGCCGCCGAGGACTTCCCCAACGGTTCAGGTTCCCCCTCAGCCACCATCTAC
ACATGCACACCAAGCTCCGAGTCTCCTGACCGCTACCTGGTGGACCACACCATCGACGGT
CGCGTCCTCTTCCCCGCCACTGGCTACCTGAGCATAGTGTGGAAGACGCTGGCCCGCGCC
TGGGCTGGGCTCGAGCAGCTGCCTGTGGTGTTTGAGGATGTGGTGCAGCACCAGGCCACC
ATCCTGCCCAAGACTGGGACAGTGTCCTTGGAGGTACGGCTCCTGGAGGCCACCGGTGCC
TTCGAGGTGTCAGAGAACGGCAACCTGGTAGTGAGTGGGAAGGTGTACCAGTGGGATGAC
CCTGACCCCAGGCTCTTCGACCACCCGGAAAGTCCCCACCCCAATTCCCCACGGAGTCCC
CTCTTCCTGGCCCAGGCAGAAGTTTACAAGGAGCTGCGTCTGCGTGGCTACGACTACGGC
CCTCATTTCCAGGGCATCCTGGAGGCCAGCCTGGAAGGTGACTCGGGGAGGCTGCTGTGG
AAGGATAACTGGGTGAGCTTCATGGACACCATGCTGCAGATGTCCATCCTGGGCTCGGCC
AAGCACGGCCTGTACCTACCCACCCGTGTCACCGCCATCCACATCGACCCTGCCACCCAC
AGGCAGAAGCTGTACACACTGCAGGACAAGGCCCAAGTGGCTGACGTGGTGGTGAGCAGG
TGGCCGAGGGTCACAGTGGCGGGAGGCGTCCACATCTCCGGGCTCCACACTGAGTCGGCC
CCGCGGCGGCACGAGGAGCAGCAGGTGCCCATCCTGGAGAAGTTTTGCTTCACTCCCCAC
ACGGAGGAGGGGTGCCTGTCTGAGCACGCTGCCCTCGAGGAGGAGCTGCAACTGTGCAAG
GGGCTGGTCGAGGCACTCGAGACCAAGGTGACCCAGCAGGGGCTGAAGATGGTGGTGCCG
GACTGGACGGGGCCCAGATCCCCCCGGGACCCCTCACAGCAGGAACTGCCCCGGCTGTTG
TCGGCTGCCTGCAGGCTTCAGCTCAACGGGAACCTGCAGCTGGAGCTGGCGCAGGTGCTG
GCCCAGGAGAGGCCCAAGCTGCCAGAGGACCCTCTGCTCAGCGGCCTCCTGGACTCCCCG
GCACTCAAGGCCTGCCTGGACACTGCCGTGGAGAACATGCCCAGCCTGAAGATGAAGGTG
GTGGAGGTGCTGGCCGGCCACGGTCACCTGTATTCCCGCATCCCAGGCCTGCTCAGCCCC
CATCCCCTGCTGCAGCTGAGCTACACGGCCACCGACCGCCACCCCCAGGCCCTGGAGGCT
GCCCAGGCCGAGCTGCAGCAGCACGACGTTGCCCAGGGCCAGTGGGATCCCGCAGACCCT
GCCCCCAGCGCCCTGGGCAGCGCGGACCTCCTGGTGTGCAACTGTGCTGTGGCTGCCCTC
GGGGACCCGGCCTCAGCTCTCAGCAACATGGTGGCTGCCCTGAGAGAAGGGGGCTTTCTG
CTCCTGCACACACTGCTCCGGGGGCACCCTCGGGACATCGTGGCCTTCCTCACCTCCACT
GAGCCGCAGTATGGCCAGGGCATCCTGAGCCAGGACGCGTGGGAGAGCCTCTTCTCCAGG
GTGTCGCTGCGCCTGGTGGGCCTGAAGAAGTCCTTCTACGGCGCCACGCTCTTCCTGTGC
CGCCGGCCCACCCCGCAGGACAGCCCCATCTTCCTGCCGGTGGACGATACCAGCTTCCGC
TGGGTGGAGTCTCTGAAGGGCATCCTGGCTGACGAAGACTCTTCCCGGCCTGTGTGGCTG
AAGGCCATCAACTGTGCCACCTCGGGCGTGGTGGGCTTGGTGAACTGTCTCCGCCGAGAG
CCCGGCGGAACCGTCCGGTGTGTGCTGCTCTCCAACCTCAGCAGCACCTCCCACGTCCCG
GAGGTGGACCCGGGCTCCGCAGAACTGCAGAAGGTGTTGCAGGGAGACCTGGTGATGAAC
GTCTACCGCGACGGGGCCTGGGGGGTTTTCCGCCACTTCCTGCTGGAGGACAAGCCTGAG
GAGCCGACGGCACATGCCTTTGTGAGCACCCTCACCCGGGGGGACCTGTCCTCCATCCGC
TGGGTCTGCTCCTCGCTGCGCCATGCCCAGCCCACCTGCCCTGGCGCCCAGCTCTGCACG
GTCTACTACGCCTCCCTCAACTTCCGCGACATCATGCTGGCCACTGGCAAGCTGTCCCCT
GATGCCATCCCAGGGAAGTGGACCTCCCAGGACAGCCTGCTAGGTATGGAGTTCTCGGGC
CGAGACGCCAGCGGCAAGCGTGTGATGGGACTGGTGCCTGCCAAGGGCCTGGCCACCTCT
GTCCTGCTGTCACCGGACTTCCTCTGGGATGTGCCTTCCAACTGGACGCTGGAGGAGGCG
GCCTCGGTGCCTGTCGTCTACAGCACGGCCTACTACGCGCTGGTGGTGCGTGGGCGGGTG
CGCCCCGGGGAGACGCTGCTCATCCACTCGGGCTCGGGCGGCGTGGGCCAGGCCGCCATC
GCCATCGCCCTCAGTCTGGGCTGCCGCGTCTTCACCACCGTGGGGTCGGCTGAGAAGCGG
GCGTACCTCCAGGCCAGGTTCCCCCAGCTCGACAGCACCAGCTTCGCCAACTCCCGGGAC
ACATCCTTCGAGCAGCATGTGCTGTGGCACACGGGCGGGAAGGGCGTTGACCTGGTCTTG
AACTCCTTGGCGGAAGAGAAGCTGCAGGCCAGCGTGAGGTGCTTCGGTACGCACGGTCGC
TTCCTGGAAATTGGCAAATTCGACCTTTCTCAGAACCACCCGCTCGGCATGGCTATCTTC
CTGAAGAACGTGACATTCCACGGGGTCCTACTGGATGCGTTCTTCAACGAGAGCAGTGCT
GACTGGCGGGAGGTGTGGGCGCTTGTCGAGGCCGCCATCCGGGATGGGGTGGTACGGCCC
CTCAAGTGCACGGTGTTCCATGGGGCCCAGGTGGAGGACGCCTTCCGCTACATGGCCCAA
GGGAAGCACATTGGCAAAGTCGTCGTGCAGGTGCTTGCGGAGGAGCCGGCAGTGCTGAAG
GGGGCCAAACCCAAGCTGATGTCGGCCATCTCCAAGACCTTCTGCCCGGCCCACAAGAGC
TACATCATCGCTGGTGGTCTGGGTGGCTTCGGCCTGGAGTTGGCGCAGTGGCTGATACAG
CGTGGGGTGCAGAAGCTCGTGTTGACTTCTCGCTCCGGGATCCGGACAGGCTACCAGGCC
AAGCAGGTCCGCCGGTGGAGGCGCCAGGGGCTACAGGTGCAGGTGTCCACCAGCAACATC
AGCTCACTGGAGGGGGCCCGGGGCCTCATTGCCGAGGCGGCGCAGCTTGGGCCCGTGGGG
GGCGTCTTCAACCTGGCCGTGGTCTTGAGAGATGGCTTGCTGGAGAACCAGACCCCAGAG
TTCTTCCAGGACGTCTGCAAGCCCAAGTACAGCGGCACCCTGAACCTGGACAGGGTGACC
CGAGAGGCGTGCCCTGAGCTGGACTACTTTGTGGTCTTCTCCTCTGTGAGCTGCGGGCGT
GGCAATGCGGGACAGAGCAACTACGGCTTTGCCAATTCCGCCATGGAGCGTATCTGTGAG
AAACGCCGGCACGAAGGCCTCCCAGGCCTGGCCGTGCAGTGGGGCGCCATCGGCACCGTG
GGCATTTTGGTGGAGACGATGAGCACCAACGACACGATCGTCAGTGGCACGCTGCCCACG
CGCATTGGCGTCCTTGGCCTGGAGGTGCTGGACCTCTTCCTGAACCAGCCCCACATGGTC
CTGAGCAGCTTTGTGCTGGCTGAGAAGGCTGCGGCCTATAGGGACAGGGACAGCCAGCGG
GACCTGGTGGAGGCCGTGGCACACATCCTGGGCATCCGCGACTTGGCTGCTGTCAACCTG
GGCGGCTCACTGGCGGACCTGGGCCTGGACTCGCTCATGAGCGCGCCGGTGCGCCAGACG
CTGGAGCGTGAGCTCAACCTGGTGCTGTCCGTGCGCGAGGTGCGGCAACTCACGCTCCGG
AAACTGCAGGAGCTGTCCTCAAAGGCGGATGAAGCCAGCGAGCTGGCATGCCCCACGCCC
AAGGAGGATGGTCTGGCCCAGCAGCAGACTCAGCTGAACCTGCGCTCCCTGCTGGTGAAA
CCGGAGGGCCCCACCCTGATGCGGCTCAACTCCGTGCAGAGCTCGGAGCGGCCCCTGTTC
CTGGTGCACCCAATCGAGGCTACCACCGTGTTCCACAGCCTCGGTCCCGGTCTCAGCATC
CCCACCTATGGCCTGCAGTGCACCCCGGCTGCGCCCCTTGACAGCATCCACAGCCTGGCT
GCCTACTACATCGACTGCATCAGGCAGGTGCAGCCCGAGGGCCCCTACCGCGTGGCCGGC
TACTCCTACGGGGCCTGCGTGGCCTTTGAAATGTGCTCCCAGCTGCAGGCCCAGCAGAGC
CCAGCCCCCACCCACAACAGCCTCTTCCTGTTCGACGGCTCGCCCACCTACGTACTGGCC
TACACCCAGAGCTACCGGGCAAAGCTGACCCCAGGCTGTAAGGCTGAGGCTGAGACGGAG
GCCATATGCTTCTTCGTGCAGCAGTTCACGGACATGGAGCACAACAGGGTGCTGGAGGCG
CTGCTGCCGCTGAAGGGCCTAGAGGAGCGTGTGGCAGCCGCCGTGGACCTGATCATCAAG
AGCCACCAGGGCCTGGACCGCCAGGAGCTGAGCTTTGCGGCCCGGTCCTTCTACTACAGG
CTGCGTGCCGCTGACCAGTATACACCCAAGGCCAAGTACAGTGGCAACGTGATGCTACTG
CGGGCCAAGACGGGTGGCCGCTACGGCGAGGACCTGGGCGCGGACTACAACCTCTCCCAG
GTATGCGACGGGAAAGTATCCGTCCATATCATCGAGGGTGACCACCGCACGCTGCTGGAG
GGCAGCGGCCTGGAGTCCATCATCAGCATCATCCACAGCTCCCTGGCTGAGCCACGTGTG
AGTCGGGAGGGCTAG
Target 2 GenBank Gene ID
Target 2 GeneCard ID FASN Link Image
Target 2 GenAtlas ID FASN Link Image
Target 2 HGNC ID HGNC:3594 Link Image
Target 2 Chromosome Location 17
Target 2 Locus 17q25
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Jayakumar A, Tai MH, Huang WY, al-Feel W, Hsu M, Abu-Elheiga L, Chirala SS, Wakil SJ: Human fatty acid synthase: properties and molecular cloning. Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8695-9. [PubMed Link Image]
  2. Semenkovich CF, Coleman T, Fiedorek FT Jr: Human fatty acid synthase mRNA: tissue distribution, genetic mapping, and kinetics of decay after glucose deprivation. J Lipid Res. 1995 Jul;36(7):1507-21. [PubMed Link Image]
  3. Kuhajda FP, Jenner K, Wood FD, Hennigar RA, Jacobs LB, Dick JD, Pasternack GR: Fatty acid synthesis: a potential selective target for antineoplastic therapy. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6379-83. [PubMed Link Image]
Target 2 Drug References
  1. Boshoff HI, Mizrahi V, Barry CE 3rd: Effects of pyrazinamide on fatty acid synthesis by whole mycobacterial cells and purified fatty acid synthase I. J Bacteriol. 2002 Apr;184(8):2167-72. [PubMed Link Image]
  2. Schroeder EK, de Souza N, Santos DS, Blanchard JS, Basso LA: Drugs that inhibit mycolic acid biosynthesis in Mycobacterium tuberculosis. Curr Pharm Biotechnol. 2002 Sep;3(3):197-225. [PubMed Link Image]
  3. Ngo SC, Zimhony O, Chung WJ, Sayahi H, Jacobs WR Jr, Welch JT: Inhibition of isolated Mycobacterium tuberculosis fatty acid synthase I by pyrazinamide analogs. Antimicrob Agents Chemother. 2007 Jul;51(7):2430-5. Epub 2007 May 7. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.