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Showing drug card for Guanidine (DB00536)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-04-16 16:47:47
Primary Accession Number DB00536
Secondary Accession Number
  • APRD01008
  • EXPT01546
Name Guanidine
Drug Type
  • Approved
  • Small Molecule
Description A strong organic base existing primarily as guanidium ions at physiological pH. It is found in the urine as a normal product of protein metabolism. It is also used in laboratory research as a protein denaturant. (From Martindale, the Extra Pharmacopoeia, 30th ed and Merck Index, 12th ed) It is also used in the treatment of myasthenia and as a fluorescent probe in HPLC. [PubChem]
Synonyms
  1. Aminomethanamidine
  2. Carbamamidine
  3. Carbamidine
  4. Guanidin
  5. Guanidine Hydrochloride
  6. Guanidinium Chloride
  7. Guanidinium Sulfate
  8. Imidourea
  9. Iminourea
Brand Names
  1. Guanidine hydrochloride
Brand Mixtures Not Available
Chemical IUPAC Name guanidine
Chemical Formula CH5N3
Chemical Structure Structure
CAS Registry Number 113-00-8
InChI Identifier InChI=1/CH5N3/c2-1(3)4/h(H5,2,3,4)/f/h2H,3-4H2
InChI Key ZRALSGWEFCBTJO-HLDZQYPKCN
KEGG Drug Not Available
KEGG Compound Not Available
PubChem Compound 3520 Link Image
PubChem Substance 218736 Link Image
ChEBI ID 24435 Link Image
PharmGKB ID PA449827 Link Image
HET ID GAI Link Image
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link Not Available
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Guanidine Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 59.0705
Monoisotopic Molecular Weight 59.0483
State Solid
Melting Point 50 oC
Experimental Water Solubility 500 mg/mL (HCl salt) Source: PhysProp
Predicted Water Solubility 1.15e+01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -0.6 Source: PhysProp
Predicted LogP -1.91 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -0.71 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point 12.5
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 1KP2 Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES NC(N)=N
Canonical SMILES NC(N)=N
Drug Category
  • Parasympathomimetics
ATC Codes
AHFS Codes Not Available
Indication For the reduction of the symptoms of muscle weakness and easy fatigability associated with the myasthenic syndrome of Eaton-Lambert. It is not indicated for treating myasthenia gravis.
Pharmacology Guanidine apparently acts by enhancing the release of acetylcholine following a nerve impulse. It also appears to slow the rates of depolarization and repolarization of muscle cell membranes.
Mechanism of Action Not Available
Absorption Rapidly absorbed and distributed
Toxicity LD50 = 475 mg/kg (oral, rat). Can cause severe gastrointestinal symptoms (nausea, vomiting and diarrhea), bone marrow suppression, renal insufficiency and other hematologic abnormalities (anemia, leucopenia). Severe guanidine intoxication is characterized by nervous hyperirritability, fibrillary tremors and convulsive contractions of muscle, salivation, vomiting, diarrhea, hypoglycemia, and circulatory disturbances.
Protein Binding Not Available
Biotransformation Not metabolized.
Half Life 7-8 hours
Dosage Forms Not Available
Patient Information Not Available
Contraindications Show Link Image
Interactions Not Available
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Aldehyde dehydrogenase, mitochondrial
  2. DNA
  3. Lysozyme
  4. Ribonuclease pancreatic
  5. Discs large homolog 4
  6. Argininosuccinate synthase
  7. Guanidinoacetate N-methyltransferase
  8. Divalent-cation tolerance protein cutA
  9. Arginase
Drug Target 1 [top]
Target 1 ID 147
Target 1 Name Aldehyde dehydrogenase, mitochondrial
Target 1 Synonyms
  1. ALDH class 2
  2. ALDH-E2
  3. ALDHI
  4. Aldehyde dehydrogenase, mitochondrial precursor
  5. EC 1.2.1.3
Target 1 Gene Name ALDH2
Target 1 Protein Sequence >Aldehyde dehydrogenase, mitochondrial precursor 
MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPS
TGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLA
ALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCG
QIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPG
FGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADM
DWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGP
QVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGP
VMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQS
PFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
Target 1 Number of Residues 525
Target 1 Molecular Weight 56382
Target 1 Theoretical pI 7.05
Target 1 GO Classification
Function
catalytic activity
oxidoreductase activity
Process
physiological process
metabolism
Component
Not Available
Target 1 General Function Energy production and conversion
Target 1 Specific Function Not Available
Target 1 Pathways
Name SMPDB Link KEGG Link
1,2-Dichloroethane degradation map00631 Link Image
Arginine and proline metabolism SMP00020 Link Image map00330 Link Image
Ascorbate and aldarate metabolism map00053 Link Image
Bile acid biosynthesis SMP00035 Link Image map00120 Link Image
Butanoate metabolism map00650 Link Image
Fatty acid metabolism SMP00051 Link Image map00071 Link Image
Glycerolipid metabolism SMP00039 Link Image map00561 Link Image
Glycolysis / Gluconeogenesis map00010 Link Image
Histidine metabolism SMP00044 Link Image map00340 Link Image
Limonene and pinene degradation map00903 Link Image
Lysine degradation SMP00037 Link Image map00310 Link Image
Propanoate metabolism SMP00016 Link Image map00640 Link Image
Pyruvate metabolism SMP00060 Link Image map00620 Link Image
Tryptophan metabolism SMP00063 Link Image map00380 Link Image
Valine, leucine and isoleucine degradation SMP00032 Link Image map00280 Link Image
beta-Alanine metabolism SMP00007 Link Image map00410 Link Image
Target 1 Reactions
  • an aldehyde + NAD+ + H2O = an acid + NADH + H+
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 28606 Link Image
Target 1 UniProtKB/Swiss-Prot ID P05091 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name ALDH2_HUMAN Link Image
Target 1 PDB ID 1OF7 Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Mitochondrion
  • mitochondrial matrix
Target 1 Gene Sequence >1551 bp 
ATGTTGCGCGCTGCCGCCGCTCGGGCCCCGCCTGGCCGCCGCCTCTTGTCAGCCGCCGCC
ACCCAGGCCGTGCCTGCCCCCAACCAGCAGCCCGAGGTCTTCTGCAACCAGATTTTCATA
AACAATGAATGGCACGATGCCGTCAGCAGGAAAACATTCCCCACCGTCAATCCGTCCACT
GGAGAGGTCATCTGTCAGGTAGCTGAAGGGGACAAGGAAGATGTGGACAAGGCACGTGAA
GGCCGCCCGGGCGCCTTCCAGCTGGGCTCACCTTGGCGCCGCATGGACGCATCACACAGC
GGCCGGCTGCTGAACCGCCTGGCCGATCTGATCGAGCGGGACCGGACCTACCTGGCGGCC
TTGGAGACCCTGGACAATGGCAAGCCCTATGTCATCTCCTACCTGGTGGATTTGGACATG
GTCCTCAAATGTCTCCGGTATTATGCCGGCTGGGCTGATAAGTACCACGGGAAAACCATC
CCCATTGACGGAGACTTCTTCAGCTACACACGCCATGAACCTGTGGGGGTGTGCGGGCAG
ATCATTCCGTGGAATTTCCCGCTCCTGATGCAAGCATGGAAGCTGGGCCCAGCCTTGGCA
ACTGGAAACGTGGTTGTGATGAAGGTAGCTGAGCAGACACCCCTCACCGCCCTCTATGTG
GCCAACCTGATCAAGGAGGCTGGCTTTCCCCCTGGTGTGGTCAACATTGTGCCTGGATTT
GGCCCCACGGCTGGGGCCGCCATTGCCTCCCATGAGGATGTGGACAAAGTGGCATTCACA
GGCTCCACTGAGATTGGCCGCGTAATCCAGGTTGCTGCTGGGAGCAGCAACCTCAAGAGA
GTGACCTTGGAGCTGGGGGGGAAGAGCCCCAACATCATCATGTCAGATGCCGATATGGAT
TGGGCCGTGGAACAGGCCCACTTCGCCCTGTTCTTCAACCAGGGCCAGTGCTGCTGTGCC
GGCTCCCGGACCTTCGTGCAGGAGGACATCTATGATGAGTTTGTGGTGCGGAGCGTTGCC
CGGGCCAAGTCTCGGGTGGTCGGGAACCCCTTTGATAGCAAGACCGAGCAGGGGCCGCAG
GTGGATGAAACTCAGTTTAAGAAGATCCTCGGCTACATCAACACGGGGAAGCAAGAGGGG
GCGAAGCTGCTGTGTGGTGGGGGCATTGCTGCTGACCGTGGTTACTTCATCCAGCCCACT
GTGTTTGGAGATGTGCAGGATGGCATGACCATCGCCAAGGAGGAGATCTTCGGGCCAGTG
ATGCAGATCCTGAAGTTCAAGACCATAGAGGAGGTTGTTGGGAGAGCCAACAATTCCACG
TACGGGCTGGCCGCAGCTGTCTTCACAAAGGATTTGGACAAGGCCAATTACCTGTCCCAG
GCCCTCCAGGCGGGCACTGTGTGGGTCAACTGCTATGATGTGTTTGGAGCCCAGTCACCC
TTTGGTGGCTACAAGATGTCGGGGAGTGGCCGGGAGTTGGGCGAGTACGGGCTGCAGGCA
TACACTGAAGTGAAAACTGTCACAGTCAAAGTGCCTCAGAAGAACTCATAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID ALDH2 Link Image
Target 1 GenAtlas ID ALDH2 Link Image
Target 1 HGNC ID HGNC:404 Link Image
Target 1 Chromosome Location 12
Target 1 Locus 12q24.2
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Ni L, Zhou J, Hurley TD, Weiner H: Human liver mitochondrial aldehyde dehydrogenase: three-dimensional structure and the restoration of solubility and activity of chimeric forms. Protein Sci. 1999 Dec;8(12):2784-90. [PubMed Link Image]
  2. Hsu LC, Bendel RE, Yoshida A: Genomic structure of the human mitochondrial aldehyde dehydrogenase gene. Genomics. 1988 Jan;2(1):57-65. [PubMed Link Image]
  3. Hsu LC, Tani K, Fujiyoshi T, Kurachi K, Yoshida A: Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3771-5. [PubMed Link Image]
  4. Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Isolation and sequence analysis of a full length cDNA clone coding for human mitochondrial aldehyde dehydrogenase. Nucleic Acids Res. 1987 Apr 10;15(7):3179. [PubMed Link Image]
  5. Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Evidence for a signal peptide at the amino-terminal end of human mitochondrial aldehyde dehydrogenase. FEBS Lett. 1987 May 11;215(2):233-6. [PubMed Link Image]
  6. Agarwal DP, Goedde HW: Human aldehyde dehydrogenase isozymes and alcohol sensitivity. Isozymes Curr Top Biol Med Res. 1987;16:21-48. [PubMed Link Image]
  7. Hempel J, Hoog JO, Jornvall H: Mitochondrial aldehyde dehydrogenase. Homology of putative targeting sequence to that of carbamyl phosphate synthetase I revealed by correlation of cDNA and protein data. FEBS Lett. 1987 Sep 28;222(1):95-8. [PubMed Link Image]
  8. Yoshida A, Ikawa M, Hsu LC, Tani K: Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases. Alcohol. 1985 Jan-Feb;2(1):103-6. [PubMed Link Image]
  9. Hempel J, Kaiser R, Jornvall H: Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations. Eur J Biochem. 1985 Nov 15;153(1):13-28. [PubMed Link Image]
  10. Yoshida A, Huang IY, Ikawa M: Molecular abnormality of an inactive aldehyde dehydrogenase variant commonly found in Orientals. Proc Natl Acad Sci U S A. 1984 Jan;81(1):258-61. [PubMed Link Image]
  11. 8561277 Novoradovsky A, Tsai SJ, Goldfarb L, Peterson R, Long JC, Goldman D: Mitochondrial aldehyde dehydrogenase polymorphism in Asian and American Indian populations: detection of new ALDH2 alleles. Alcohol Clin Exp Res. 1995 Oct;19(5):1105-10.
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 874
Target 2 Name DNA
Target 2 Synonyms
  1. Deoxyribonucleic acid
Target 2 Gene Name Not Available
Target 2 Protein Sequence Not Available
Target 2 Number of Residues 0
Target 2 Molecular Weight 7656 (double strand)
Target 2 Theoretical pI Not Available
Target 2 GO Classification
Function
information storage
information transfer
Process
DNA replication and chromosomal cycle
DNA replication
DNA-dependent DNA replication
DNA replication, synthesis of RNA primer
transcription
transcription, DNA dependent
Component
cell
intracellular
nucleus
mitochondria
Target 2 General Function Biological information storage and information transfer
Target 2 Specific Function DNA is the molecule of heredity, as it is responsible for the genetic propagation of most inherited traits. It is a polynucleic acid that carries genetic information on cell growth, division, and function. DNA consists of two long strands of nucleotides twisted into a double helix and held together by hydrogen bonds. The sequence of nucleotides determines hereditary characteristics. Each strand serves as the template for subsequent DNA replication and as a template for mRNA production, leading to protein synthesis via ribosomes.
Target 2 Pathways
Name SMPDB Link KEGG Link
DNA polymerase map03030 Link Image
RNA polymerase map03020 Link Image
Target 2 Reactions
  • DNA + DNA polymerase + nNTP = 2 DNA + nNDP; DNA + RNA polymerase + NTP = mRNA + nNDP
Target 2 Pfam Domain Function Not Available
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Essential
Target 2 GenBank ID Protein Not Available
Target 2 UniProtKB/Swiss-Prot ID Not Available
Target 2 UniProtKB/Swiss-Prot Entry Name Not Available
Target 2 PDB ID 1BNA Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Nucleus and mitochondria
Target 2 Gene Sequence >Example: Dickerson dodecamer 
CGCGAATTCGCG
Target 2 GenBank Gene ID
Target 2 GeneCard ID Not Available
Target 2 GenAtlas ID Not Available
Target 2 HGNC ID Not Available
Target 2 Chromosome Location Not Available
Target 2 Locus All loci
Target 2 SNPs Not Available
Target 2 General References
  1. Nadeau D, Marchand C: Change in the kinetics of sulphacetamide tissue distribution in Walker tumor-bearing rats. Drug Metab Dispos. 1975 Nov-Dec;3(6):565-76. [PubMed Link Image]
Target 2 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 3 [top]
Target 3 ID 2300
Target 3 Name Lysozyme
Target 3 Synonyms
  1. EC 3.2.1.17
  2. Endolysin
  3. Lysis protein
  4. Muramidase
Target 3 Gene Name E
Target 3 Protein Sequence >Lysozyme 
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITK
DEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRM
LQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYKNL
Target 3 Number of Residues 166
Target 3 Molecular Weight 18636
Target 3 Theoretical pI 10.08
Target 3 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on glycosyl bonds
hydrolase activity, hydrolyzing O-glycosyl compounds
lysozyme activity
Process
catabolism
cellular catabolism
cell wall catabolism
physiological process
metabolism
macromolecule metabolism
carbohydrate metabolism
cellular carbohydrate metabolism
peptidoglycan metabolism
peptidoglycan catabolism
Component
Not Available
Target 3 General Function Involved in lysozyme activity
Target 3 Specific Function Helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan
Target 3 Pathways Not Available
Target 3 Reactions
  • Hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Essential
Target 3 GenBank ID Protein 15261 Link Image
Target 3 UniProtKB/Swiss-Prot ID P00720 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name LYS_BPT4 Link Image
Target 3 PDB ID 7LZM Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location
  • Cytoplasmic
Target 3 Gene Sequence >495 bp 
ATGAATATATTTGAAATGTTACGTATAGATGAACGTCTTAGACTTAAAATCTATAAAGAC
ACAGAAGGCTATTACACTATTGGCATCGGTCATTTGCTTACAAAAAGTCCATCACTTAAT
GCTGCTAAATCTGAATTAGATAAAGCTATTGGGCGTAATTGCAATGGTGTAATTACAAAA
GATGAGGCTGAAAAACTCTTTAATCAGGATGTTGATGCTGCTGTTCGCGGAATTCTGAGA
AATGCTAAATTAAAACCGGTTTATGATTCTCTTGATGCGGTTCGTCGCTGTGCATTGATT
AATATGGTTTTCCAAATGGGAGAAACCGGTGTGGCAGGATTTACTAACTCTTTACGTATG
CTTCAACAAAAACGCTGGGATGAAGCAGCAGTTAACTTAGCTAAAAGTATATGGTATAAT
CAAACACCTAATCGCGCAAAACGAGTCATTACAACGTTTAGAACTGGCACTTGGGACGCG
TATAAAAATCTATAA
Target 3 GenBank Gene ID
Target 3 GeneCard ID Not Available
Target 3 GenAtlas ID Not Available
Target 3 HGNC ID Not Available
Target 3 Chromosome Location Not Available
Target 3 Locus Not Available
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Miller ES, Kutter E, Mosig G, Arisaka F, Kunisawa T, Ruger W: Bacteriophage T4 genome. Microbiol Mol Biol Rev. 2003 Mar;67(1):86-156, table of contents. [PubMed Link Image]
  2. Eriksson AE, Baase WA, Wozniak JA, Matthews BW: A cavity-containing mutant of T4 lysozyme is stabilized by buried benzene. Nature. 1992 Jan 23;355(6358):371-3. [PubMed Link Image]
  3. McIntosh LP, Wand AJ, Lowry DF, Redfield AG, Dahlquist FW: Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme. Biochemistry. 1990 Jul 10;29(27):6341-62. [PubMed Link Image]
  4. Faber HR, Matthews BW: A mutant T4 lysozyme displays five different crystal conformations. Nature. 1990 Nov 15;348(6298):263-6. [PubMed Link Image]
  5. Valerie K, Stevens J, Lynch M, Henderson EE, de Riel JK: Nucleotide sequence and analysis of the 58.3 to 65.5-kb early region of bacteriophage T4. Nucleic Acids Res. 1986 Nov 11;14(21):8637-54. [PubMed Link Image]
  6. Remington SJ, Eyck LF, Matthews BW: Atomic coordinates for T4 phage lysozyme. Biochem Biophys Res Commun. 1977 Mar 21;75(2):265-70. [PubMed Link Image]
  7. Matsumura M, Becktel WJ, Matthews BW: Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. Nature. 1988 Aug 4;334(6181):406-10. [PubMed Link Image]
  8. Weaver LH, Matthews BW: Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution. J Mol Biol. 1987 Jan 5;193(1):189-99. [PubMed Link Image]
  9. Matthews BW, Remington SJ: The three dimensional structure of the lysozyme from bacteriophage T4. Proc Natl Acad Sci U S A. 1974 Oct;71(10):4178-82. [PubMed Link Image]
  10. Inouye M, Imada M, Tsugita A: The amino acid sequence of T4 phage lysozyme. IV. Dilute acid hydrolysis and the order of tryptic peptides. J Biol Chem. 1970 Jul 25;245(14):3479-84. [PubMed Link Image]
  11. 6302287 Owen JE, Schultz DW, Taylor A, Smith GR: Nucleotide sequence of the lysozyme gene of bacteriophage T4. Analysis of mutations involving repeated sequences. J Mol Biol. 1983 Apr 5;165(2):229-48.
Target 3 Drug References
  1. Shiraki K, Kudou M, Sakamoto R, Yanagihara I, Takagi M: Amino Acid esters prevent thermal inactivation and aggregation of lysozyme. Biotechnol Prog. 2005 Mar-Apr;21(2):640-3. [PubMed Link Image]
  2. Junn HJ, Youn J, Suh KH, Lee SS: Cloning and expression of Klebsiella phage K11 lysozyme gene. Protein Expr Purif. 2005 Jul;42(1):78-84. Epub 2005 Apr 19. [PubMed Link Image]
  3. Garcia-Orozco KD, Lopez-Zavala AA, Puentes-Camacho D, Calderon-de-la-Barca AM, Sotelo-Mundo RR: Recombinant bacterial expression of the lysozyme from the tobacco-hornworm Manduca sexta with activity at low temperatures. Biotechnol Lett. 2005 Aug;27(15):1075-80. [PubMed Link Image]
  4. 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]
  5. 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 4 [top]
Target 4 ID 2496
Target 4 Name Ribonuclease pancreatic
Target 4 Synonyms
  1. EC 3.1.27.5
  2. RNase 1
  3. RNase A
  4. Ribonuclease pancreatic precursor
Target 4 Gene Name RNASE1
Target 4 Protein Sequence >Ribonuclease pancreatic precursor 
MALKSLVLLSLLVLVLLLVRVQPSLGKETAAAKFERQHMDSSTSAASSSNYCNQMMKSRN
LTKDRCKPVNTFVHESLADVQAVCSQKNVACKNGQTNCYQSYSTMSITDCRETGSSKYPN
CAYKTTQANKHIIVACEGNPYVPVHFDASV
Target 4 Number of Residues 152
Target 4 Molecular Weight 16461
Target 4 Theoretical pI 8.74
Target 4 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on ester bonds
nuclease activity
endonuclease activity
endoribonuclease activity
endoribonuclease activity, producing 3'-phosphomonoesters
pancreatic ribonuclease activity
binding
nucleic acid binding
Process
Not Available
Component
Not Available
Target 4 General Function Involved in nucleic acid binding
Target 4 Specific Function Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA
Target 4 Pathways Not Available
Target 4 Reactions
  • Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates REFERENCE 1 AUTHORS Anfinsen, C.B. and White, F.H., Jr. TITLE The ribonucleases: occurrence, structure, and properties. JOURNAL In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 5, Academic Press, New York, 1961, p. 95-122. REFERENCE 2 [PMID:14247667] AUTHORS BEARD JR, RAZZELL WE. TITLE PURIFICATION OF ALKALINE RIBONUCLEASE II FROM MITOCHONDRIAL AND SOLUBLE FRACTIONS OF LIVER. JOURNAL J. Biol. Chem. 239 (1964) 4186-93. ORGANISM pig [GN:ssc], rat [GN:rno], cow [GN:bta]
Target 4 Pfam Domain Function
Target 4 Signals
  • 1-26
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Essential
Target 4 GenBank ID Protein 672 Link Image
Target 4 UniProtKB/Swiss-Prot ID P61823 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name RNAS1_BOVIN Link Image
Target 4 PDB ID 1C0B Link Image
Target 4 PDB File Show
Target 4 3D Structure
Target 4 Cellular Location
  • Secreted protein
Target 4 Gene Sequence >453 bp 
ATGGCTCTGAAGTCCCTGGTCCTGTTGTCGCTGTTGGTCCTGGTGCTGCTGCTGGTGCGG
GTCCAGCCTTCCCTGGGCAAGGAAACTGCAGCAGCCAAGTTTGAGCGGCAGCACATGGAC
TCCAGCACTTCCGCTGCCAGCAGCTCCAACTACTGTAACCAGATGATGAAGAGCCGGAAC
CTGACCAAAGATCGATGCAAGCCAGTGAACACCTTTGTGCACGAGTCCCTGGCTGATGTC
CAGGCCGTGTGCTCCCAGAAAAATGTTGCCTGCAAGAATGGGCAGACCAATTGCTACCAG
AGCTACTCCACCATGAGCATCACCGACTGCCGTGAGACCGGCAGCTCCAAGTACCCCAAC
TGTGCCTACAAGACCACCCAGGCGAATAAACACATCATTGTGGCTTGTGAGGGAAACCCG
TACGTGCCAGTCCACTTTGATGCTTCAGTGTAG
Target 4 GenBank Gene ID
Target 4 GeneCard ID Not Available
Target 4 GenAtlas ID Not Available
Target 4 HGNC ID Not Available
Target 4 Chromosome Location Not Available
Target 4 Locus Not Available
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Rico M, Santoro J, Gonzalez C, Bruix M, Neira JL, Nieto JL, Herranz J: 3D structure of bovine pancreatic ribonuclease A in aqueous solution: an approach to tertiary structure determination from a small basis of 1H NMR NOE correlations. J Biomol NMR. 1991 Sep;1(3):283-98. [PubMed Link Image]
  2. Robertson AD, Purisima EO, Eastman MA, Scheraga HA: Proton NMR assignments and regular backbone structure of bovine pancreatic ribonuclease A in aqueous solution. Biochemistry. 1989 Jul 11;28(14):5930-8. [PubMed Link Image]
  3. Rico M, Bruix M, Santoro J, Gonzalez C, Neira JL, Nieto JL, Herranz J: Sequential 1H-NMR assignment and solution structure of bovine pancreatic ribonuclease A. Eur J Biochem. 1989 Aug 15;183(3):623-38. [PubMed Link Image]
  4. Carsana A, Confalone E, Palmieri M, Libonati M, Furia A: Structure of the bovine pancreatic ribonuclease gene: the unique intervening sequence in the 5' untranslated region contains a promoter-like element. Nucleic Acids Res. 1988 Jun 24;16(12):5491-502. [PubMed Link Image]
  5. Wlodawer A, Svensson LA, Sjolin L, Gilliland GL: Structure of phosphate-free ribonuclease A refined at 1.26 A. Biochemistry. 1988 Apr 19;27(8):2705-17. [PubMed Link Image]
  6. McPherson A, Brayer G, Cascio D, Williams R: The mechanism of binding of a polynucleotide chain to pancreatic ribonuclease. Science. 1986 May 9;232(4751):765-8. [PubMed Link Image]
  7. Carlisle CH, Palmer RA, Mazumdar SK, Gorinsky BA, Yeates DG: The structure of ribonuclease at 2-5 Angstrom resolution. J Mol Biol. 1974 May 5;85(1):1-18. [PubMed Link Image]
  8. Wyckoff HW, Tsernoglou D, Hanson AW, Knox JR, Lee B, Richards FM: The three-dimensional structure of ribonuclease-S. Interpretation of an electron density map at a nominal resolution of 2 A. J Biol Chem. 1970 Jan 25;245(2):305-28. [PubMed Link Image]
  9. Shall S, Barnard EA: Heavy atom-labelled derivatives of bovine pancreatic ribonuclease. I. Specific reactions of ribonuclease with N-acetylhomocysteine thiolactone and silver ion. J Mol Biol. 1969 Apr;41(2):237-51. [PubMed Link Image]
  10. Wlodawer A, Bott R, Sjolin L: The refined crystal structure of ribonuclease A at 2.0 A resolution. J Biol Chem. 1982 Feb 10;257(3):1325-32. [PubMed Link Image]
  11. 7479688 delCardayre SB, Ribo M, Yokel EM, Quirk DJ, Rutter WJ, Raines RT: Engineering ribonuclease A: production, purification and characterization of wild-type enzyme and mutants at Gln11. Protein Eng. 1995 Mar;8(3):261-73.
  12. 8587129 Confalone E, Beintema JJ, Sasso MP, Carsana A, Palmieri M, Vento MT, Furia A: Molecular evolution of genes encoding ribonucleases in ruminant species. J Mol Evol. 1995 Dec;41(6):850-8.
  13. 9154942 Leonidas DD, Shapiro R, Irons LI, Russo N, Acharya KR: Crystal structures of ribonuclease A complexes with 5'-diphosphoadenosine 3'-phosphate and 5'-diphosphoadenosine 2'-phosphate at 1.7 A resolution. Biochemistry. 1997 May 6;36(18):5578-88.
Target 4 Drug References
  1. Nasiri H, Forouzandeh M, Rasaee MJ, Rahbarizadeh F: Modified salting-out method: high-yield, high-quality genomic DNA extraction from whole blood using laundry detergent. J Clin Lab Anal. 2005;19(6):229-32. [PubMed Link Image]
  2. 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]
  3. 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]
  4. Dodge RW, Laity JH, Rothwarf DM, Shimotakahara S, Scheraga HA: Folding pathway of guanidine-denatured disulfide-intact wild-type and mutant bovine pancreatic ribonuclease A. J Protein Chem. 1994 May;13(4):409-21. [PubMed Link Image]
  5. Loh SN, Rohl CA, Kiefhaber T, Baldwin RL: A general two-process model describes the hydrogen exchange behavior of RNase A in unfolding conditions. Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):1982-7. [PubMed Link Image]
Drug Target 5 [top]
Target 5 ID 2571
Target 5 Name Discs large homolog 4
Target 5 Synonyms
  1. PSD-95
  2. Postsynaptic density protein 95
  3. SAP90
  4. Synapse-associated protein 90
Target 5 Gene Name Dlg4
Target 5 Protein Sequence >Discs large homolog 4 
MDCLCIVTTKKYRYQDEDTPPLEHSPAHLPNQANSPPVIVNTDTLEAPGYELQVNGTEGE
MEYEEITLERGNSGLGFSIAGGTDNPHIGDDPSIFITKIIPGGAAAQDGRLRVNDSILFV
NEVDVREVTHSAAVEALKEAGSIVRLYVMRRKPPAEKVMEIKLIKGPKGLGFSIAGGVGN
QHIPGDNSIYVTKIIEGGAAHKDGRLQIGDKILAVNSVGLEDVMHEDAVAALKNTYDVVY
LKVAKPSNAYLSDSYAPPDITTSYSQHLDNEISHSSYLGTDYPTAMTPTSPRRYSPVAKD
LLGEEDIPREPRRIVIHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDQIL
SVNGVDLRNASHEQAAIALKNAGQTVTIIAQYKPEEYSRFEAKIHDLREQLMNSSLGSGT
ASLRSNPKRGFYIRALFDYDKTKDCGFLSQALSFRFGDVLHVIDAGDEEWWQARRVHSDS
ETDDIGFIPSKRRVERREWSRLKAKDWGSSSGSQGREDSVLSYETVTQMEVHYARPIIIL
GPTKDRANDDLLSEFPDKFGSCVPHTTRPKREYEIDGRDYHFVSSREKMEKDIQAHKFIE
AGQYNSHLYGTSVQSVREVAEQGKHCILDVSANAVRRLQAAHLHPIAIFIRPRSLENVLE
INKRITEEQARKAFDRATKLEQEFTECFSAIVEGDSFEEIYHKVKRVIEDLSGPYIWVPA
RERL
Target 5 Number of Residues 736
Target 5 Molecular Weight 80466
Target 5 Theoretical pI 5.71
Target 5 GO Classification
Function
binding
protein binding
Process
Not Available
Component
Not Available
Target 5 General Function Nucleotide transport and metabolism
Target 5 Specific Function Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ACCN3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B
Target 5 Pathways Not Available
Target 5 Reactions Not Available
Target 5 Pfam Domain Function
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • None
Target 5 Essentiality Essential
Target 5 GenBank ID Protein 206455 Link Image
Target 5 UniProtKB/Swiss-Prot ID P31016 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name DLG4_RAT Link Image
Target 5 PDB ID 1JXO Link Image
Target 5 PDB File Show
Target 5 3D Structure
Target 5 Cellular Location
  • Cell membrane
  • peripheral membrane protein. Cell membrane
  • postsynaptic densi
  • postsynaptic membrane
Target 5 Gene Sequence >2175 bp 
ATGGACTGTCTCTGTATAGTGACAACCAAGAAATACCGCTACCAAGATGAAGACACGCCC
CCTCTGGAACACAGCCCGGCCCACCTCCCCAACCAGGCCAATTCTCCCCCTGTGATTGTC
AACACGGACACCCTAGAAGCCCCAGGATATGAGTTGCAGGTGAATGGAACAGAGGGGGAG
ATGGAGTATGAGGAGATCACATTGGAAAGGGGTAACTCAGGTCTGGGCTTCAGCATCGCA
GGTGGCACTGACAACCCGCACATCGGTGACGACCCGTCCATTTTTATCACCAAGATCATT
CCTGGTGGGGCTGCAGCCCAGGATGGCCGCCTCAGGGTCAATGACAGCATCCTGTTTGTA
AATGAAGTGGATGTTCGGGAGGTGACCCATTCAGCTGCGGTGGAGGCCCTCAAAGAGGCA
GGTTCCATCGTTCGCCTCTATGTCATGCGCCGGAAACCCCCAGCCGAAAAGGTCATGGAG
ATCAAACTCATCAAAGGGCCTAAAGGACTTGGCTTCAGCATTGCGGGGGGCGTTGGGAAC
CAGCACATCCCTGGAGATAACAGCATCTATGTAACGAAGATCATCGAAGGAGGTGCTGCC
CACAAGGATGGCAGGTTGCAGATTGGAGACAAGATCCTGGCGGTCAACAGTGTGGGGCTG
GAGGACGTCATGCACGAGGATGCCGTGGCAGCCCTGAAGAACACATATGACGTTGTGTAC
CTAAAGGTGGCCAAGCCCAGCAATGCCTACCTGAGTGACAGCTATGCTCCCCCAGACATC
ACAACCTCGTATTCTCAGCACCTGGACAATGAGATCAGTCATAGCAGCTACTTGGGCACT
GACTACCCCACAGCCATGACCCCCACTTCCCCTCGGCGCTACTCCCCTGTGGCCAAGGAC
CTGCTGGGGGAGGAAGACATTCCCCGGGAACCAAGGCGGATCGTGATCCATCGGGGCTCC
ACCGGCCTGGGCTTCAACATCGTGGGCGGCGAGGATGGTGAAGGCATCTTCATCTCCTTC
ATCCTTGCTGGGGGTCCAGCCGACCTCAGTGGGGAGCTACGGAAGGGGGACCAGATCCTG
TCGGTCAATGGTGTTGACCTCCGCAATGCCAGTCACGAACAGGCTGCCATTGCCCTGAAG
AATGCGGGTCAGACGGTCACGATCATCGCTCAGTATAAACCAGAAGAGTATAGTCGATTC
GAGGCCAAGATCCATGATCTTCGGGAACAGCTCATGAATAGTAGCCTAGGCTCAGGGACT
GCATCCTTGCGAAGCAACCCCAAGAGGGGCTTCTACATTAGGGCCCTGTTTGATTACGAC
AAGACCAAGGACTGCGGTTTCTTGAGCCAGGCCCTGAGCTTCCGCTTCGGGGATGTGCTT
CATGTCATTGACGCTGGTGACGAAGAGTGGTGGCAAGCACGGCGGGTCCACTCCGACAGT
GAGACCGACGACATTGGCTTCATTCCCAGCAAACGGCGGGTCGAGCGACGAGAGTGGTCA
AGGTTAAAGGCCAAGGACTGGGGCTCCAGCTCTGGATCACAGGGTCGAGAAGACTCGGTT
CTGAGCTATGAGACGGTGACCCAGATGGAAGTGCACTATGCTCGTCCCATCATCATCCTT
GGACCCACCAAAGACCGTGCCAACGATGATCTTCTCTCCGAGTTCCCCGACAAGTTTGGA
TCCTGTGTCCCTCATACGACACGTCCTAAGCGGGAATATGAGATAGACGGCCGGGATTAC
CACTTTGTCTCCTCCCGGGAGAAAATGGAGAAGGACATCCAGGCACACAAGTTCATTGAG
GCTGGCCAGTACAACAGCCACCTCTATGGGACCAGCGTCCAGTCTGTGCGAGAGGTAGCA
GAGCAGGGGAAGCACTGCATCCTCGATGTCTCGGCCAATGCCGTGCGGCGGCTGCAGGCG
GCCCACCTGCACCCCATCGCCATCTTCATCCGTCCCCGCTCCCTGGAGAATGTGCTAGAG
ATCAATAAGCGGATCACAGAGGAGCAAGCCCGGAAAGCCTTCGACAGAGCCACGAAGCTG
GAGCAGGAGTTCACAGAGTGCTTCTCAGCCATCGTAGAGGGCGACAGCTTTGAAGAGATC
TATCACAAAGTGAAACGTGTCATTGAAGACCTCTCAGGCCCCTACATCTGGGTCCCAGCC
CGAGAGAGACTCTGA
Target 5 GenBank Gene ID
Target 5 GeneCard ID Not Available
Target 5 GenAtlas ID Not Available
Target 5 HGNC ID Not Available
Target 5 Chromosome Location Not Available
Target 5 Locus Not Available
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. Tochio H, Hung F, Li M, Bredt DS, Zhang M: Solution structure and backbone dynamics of the second PDZ domain of postsynaptic density-95. J Mol Biol. 2000 Jan 14;295(2):225-37. [PubMed Link Image]
  2. El-Husseini AE, Craven SE, Chetkovich DM, Firestein BL, Schnell E, Aoki C, Bredt DS: Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering. J Cell Biol. 2000 Jan 10;148(1):159-72. [PubMed Link Image]
  3. McGee AW, Dakoji SR, Olsen O, Bredt DS, Lim WA, Prehoda KE: Structure of the SH3-guanylate kinase module from PSD-95 suggests a mechanism for regulated assembly of MAGUK scaffolding proteins. Mol Cell. 2001 Dec;8(6):1291-301. [PubMed Link Image]
  4. Tavares GA, Panepucci EH, Brunger AT: Structural characterization of the intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95. Mol Cell. 2001 Dec;8(6):1313-25. [PubMed Link Image]
  5. Wong W, Newell EW, Jugloff DG, Jones OT, Schlichter LC: Cell surface targeting and clustering interactions between heterologously expressed PSD-95 and the Shal voltage-gated potassium channel, Kv4.2. J Biol Chem. 2002 Jun 7;277(23):20423-30. Epub 2002 Mar 28. [PubMed Link Image]
  6. Cho KO, Hunt CA, Kennedy MB: The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein. Neuron. 1992 Nov;9(5):929-42. [PubMed Link Image]
  7. Kistner U, Wenzel BM, Veh RW, Cases-Langhoff C, Garner AM, Appeltauer U, Voss B, Gundelfinger ED, Garner CC: SAP90, a rat presynaptic protein related to the product of the Drosophila tumor suppressor gene dlg-A. J Biol Chem. 1993 Mar 5;268(7):4580-3. [PubMed Link Image]
  8. Doyle DA, Lee A, Lewis J, Kim E, Sheng M, MacKinnon R: Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell. 1996 Jun 28;85(7):1067-76. [PubMed Link Image]
  9. Brenman JE, Christopherson KS, Craven SE, McGee AW, Bredt DS: Cloning and characterization of postsynaptic density 93, a nitric oxide synthase interacting protein. J Neurosci. 1996 Dec 1;16(23):7407-15. [PubMed Link Image]
  10. Takeuchi M, Hata Y, Hirao K, Toyoda A, Irie M, Takai Y: SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density. J Biol Chem. 1997 May 2;272(18):11943-51. [PubMed Link Image]
  11. 9581761 Kim JH, Liao D, Lau LF, Huganir RL: SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein family. Neuron. 1998 Apr;20(4):683-91.
  12. 9756850 Deguchi M, Hata Y, Takeuchi M, Ide N, Hirao K, Yao I, Irie M, Toyoda A, Takai Y: BEGAIN (brain-enriched guanylate kinase-associated protein), a novel neuronal PSD-95/SAP90-binding protein. J Biol Chem. 1998 Oct 9;273(41):26269-72.
Target 5 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 6 [top]
Target 6 ID 3194
Target 6 Name Argininosuccinate synthase
Target 6 Synonyms
  1. Citrulline--aspartate ligase
  2. EC 6.3.4.5
Target 6 Gene Name argG
Target 6 Protein Sequence >Argininosuccinate synthase 
MTTILKHLPVGQRIGIAFSGGLDTSAALLWMRQKGAVPYAYTANLGQPDEEDYDAIPRRA
MEYGAENARLIDCRKQLVAEGIAAIQCGAFHNTTGGLTYFNTTPLGRAVTGTMLVAAMKE
DGVNIWGDGSTYKGNDIERFYRYGLLTNAELQIYKPWLDTDFIDELGGRHEMSEFMIACG
FDYKMSVEKAYSTDSNMLGATHEAKDLEYLNSSVKIVNPIMGVKFWDESVKIPAEEVTVR
FEQGHPVALNGKTFSDDVEMMLEANRIGGRHGLGMSDQIENRIIEAKSRGIYEAPGMALL
HIAYERLLTGIHNEDTIEQYHAHGRQLGRLLYQGRWFDSQALMLRDSLQRWVASQITGEV
TLELRRGNDYSILNTVSENLTYKPERLTMEKGDSVFSPDDRIGQLTMRNLDITDTREKLF
GYAKTGLLSSSAASGVPQVENLENKGQ
Target 6 Number of Residues 454
Target 6 Molecular Weight 49899
Target 6 Theoretical pI 5.04
Target 6 GO Classification
Function
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
catalytic activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
argininosuccinate synthase activity
Process
physiological process
metabolism
urea cycle intermediate metabolism
arginine metabolism
arginine biosynthesis
Component
Not Available
Target 6 General Function Amino acid transport and metabolism
Target 6 Specific Function ATP + L-citrulline + L-aspartate = AMP + diphosphate + omega-N-(L-arginino)succinate
Target 6 Pathways
Name SMPDB Link KEGG Link
Urea cycle and metabolism of amino groups map00220 Link Image
Target 6 Reactions
  • ATP + L-citrulline + L-aspartate = AMP + diphosphate + 2-(Nomega-L-arginino)succinate
Target 6 Pfam Domain Function
Target 6 Signals
  • None
Target 6 Transmembrane Regions
  • None
Target 6 Essentiality Essential
Target 6 GenBank ID Protein 145342 Link Image
Target 6 UniProtKB/Swiss-Prot ID P0A6E4 Link Image
Target 6 UniProtKB/Swiss-Prot Entry Name ASSY_ECOLI Link Image
Target 6 PDB ID 1KP3 Link Image
Target 6 PDB File Show
Target 6 3D Structure
Target 6 Cellular Location
  • Cytoplasm (Probable)
Target 6 Gene Sequence >1344 bp 
ATGACGACGATTCTCAAGCATCTCCCGGTAGGTCAACGTATTGGTATCGCTTTTTCTGGC
GGTCTGGACACCAGTGCCGCACTGCTGTGGATGCGACAAAAGGGAGCGGTTCCTTATGCA
TATACTGCAAACCTGGGCCAGCCAGACGAAGAGGATTATGATGCGATCCCTCGTCGTGCC
ATGGAATACGGCGCGGAGAACGCACGTCTGATCGACTGCCGCAAACAACTGGTGGCCGAA
GGTATTGCCGCTATTCAGTGTGGCGCATTTCATAACACCACCGGCGGCCTGACCTATTTC
AACACGACGCCGCTGGGCCGCGCCGTGACTGGTACCATGCTGGTTGCTGCGATGAAAGAA
GATGGCGTGAATATCTGGGGTGACGGTAGCACCTACAAAGGAAACGATATCGAACGTTTC
TATCGTTATGGTCTGCTGACCAATGCTGAACTGCAGATTTACAAACCGTGGCTTGATACT
GACTTTATTGATGAACTGGGCGGCCGTCATGAGATGTCTGAATTTATGATTGCCTGCGGT
TTCGACTACAAAATGTCTGTCGAAAAAGCCTACTCCACAGACTCCAACATGCTTGGTGCA
ACGCATGAAGCGAAGGATCTGGAATACCTCAACTCCAGCGTCAAAATCGTCAACCCGAAT
ATGGGCGTGAAATTCTGGGATGAGAGCGTGAAGATCCCGGCAGAAGAAGTCACAGTACGC
TTTGAACAAGGTCATCCGGTGGCGCTGAACGGTAAAACCTTTAGCGACGACGTAGAAATG
ATGCTGGAAGCTAACCGCATCGGCGGTCGTCACGGCCTGGGCATGAGCGACCAGATTGAA
AACCGTATCATCGAAGCGAAAAGCCGTGGTATTTACGAAGCTCCGGGGATGGCACTGCTG
CACATTGCGTATGAACGCCTGTTGACCGGTATTCACAACGAAGACACCATTGAGCAGTAT
CACGCGCATGGTCGTCAGTTGGATCGCCTGCTGTACCAGGGGCGTTGGTTTGACTCCCAG
GCGCTGATGCTGCGTGACTCTCTGCAACGCTGGGTTGCCAGCCAGATCACTGGTGAAGTT
ACCCTGGAGCTGCGCCGTGGGAACGATTATTCAATCCTGAATACCGTCTCAGAGAACCTG
ACCTACAAGCCAGAGCGTCTGACGATGGAAAAAGGCGACTCGGTGTTCTCGCCAGATGAT
CGTATTGGTCAATTGACCATGCGTAACCTGGATATCACTGATACCCGCGAGAAACTTTTC
GGTTATGCCAAAACTGGCCTGCTTTCCTCCTCTGCCGCTTCAGGCGTGCCGCAGGTGGAG
AATCTGGAAAACAAAGGCCAGTAA
Target 6 GenBank Gene ID
Target 6 GeneCard ID Not Available
Target 6 GenAtlas ID Not Available
Target 6 HGNC ID Not Available
Target 6 Chromosome Location Not Available
Target 6 Locus Not Available
Target 6 SNPs SNPJam Report Link Image
Target 6 General References
  1. Lemke C, Yeung M, Howell PL: Expression, purification, crystallization and preliminary X-ray analysis of Escherichia coli argininosuccinate synthetase. Acta Crystallogr D Biol Crystallogr. 1999 Dec;55(Pt 12):2028-30. [PubMed Link Image]
  2. Lemke CT, Howell PL: The 1.6 A crystal structure of E. coli argininosuccinate synthetase suggests a conformational change during catalysis. Structure. 2001 Dec;9(12):1153-64. [PubMed Link Image]
  3. Lemke CT, Howell PL: Substrate induced conformational changes in argininosuccinate synthetase. J Biol Chem. 2002 Apr 12;277(15):13074-81. Epub 2002 Jan 23. [PubMed Link Image]
  4. Van Vliet F, Crabeel M, Boyen A, Tricot C, Stalon V, Falmagne P, Nakamura Y, Baumberg S, Glansdorff N: Sequences of the genes encoding argininosuccinate synthetase in Escherichia coli and Saccharomyces cerevisiae: comparison with methanogenic archaebacteria and mammals. Gene. 1990 Oct 30;95(1):99-104. [PubMed Link Image]
  5. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
  6. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [PubMed Link Image]
Target 6 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 7 [top]
Target 7 ID 3360
Target 7 Name Guanidinoacetate N-methyltransferase
Target 7 Synonyms
  1. EC 2.1.1.2
Target 7 Gene Name Gamt
Target 7 Protein Sequence >Guanidinoacetate N-methyltransferase 
MSSSAASPLFAPGEDCGPAWRAAPAAYDTSDTHLQILGKPVMERWETPYMHSLAAAAASR
GGRVLEVGFGMAIAASRVQQAPIKEHWIIECNDGVFQRLQNWALKQPHKVVPLKGLWEEE
APTLPDGHFDGILYDTYPLSEETWHTHQFNFIKTHAFRLLKPGGILTYCNLTSWGELMKS
KYTDITAMFEETQVPALLEAGFQRENICTEVMALVPPADCRYYAFPQMITPLVTKH
Target 7 Number of Residues 239
Target 7 Molecular Weight 26407
Target 7 Theoretical pI 6.02
Target 7 GO Classification Not Available
Target 7 General Function Involved in guanidinoacetate N-methyltransferase activity
Target 7 Specific Function S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine
Target 7 Pathways
Name SMPDB Link KEGG Link
Urea cycle and metabolism of amino groups map00220 Link Image
Target 7 Reactions
  • S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine
Target 7 Pfam Domain Function Not Available
Target 7 Signals
  • None
Target 7 Transmembrane Regions
  • None
Target 7 Essentiality Essential
Target 7 GenBank ID Protein 204436 Link Image
Target 7 UniProtKB/Swiss-Prot ID P10868 Link Image
Target 7 UniProtKB/Swiss-Prot Entry Name GAMT_RAT Link Image
Target 7 PDB ID 1XCL Link Image
Target 7 PDB File Show
Target 7 3D Structure
Target 7 Cellular Location Not Available
Target 7 Gene Sequence >711 bp 
ATGAGTTCTTCTGCAGCCAGCCCGCTTTTCGCGCCTGGCGAGGACTGCGGCCCCGCGTGG
CGCGCGGCCCCCGCGGCCTATGATACGTCTGACACGCACCTGCAGATCCTGGGCAAGCCA
GTAATGGAGCGTTGGGAGACCCCCTACATGCATTCGCTGGCGGCTGCTGCTGCCTCCAGA
GGGGGCCGGGTCCTGGAAGTGGGCTTTGGGATGGCCATTGCAGCCTCCAGGGTGCAGCAG
GCCCCCATAAAGGAACACTGGATTATTGAATGCAACGATGGGGTCTTCCAGCGTCTACAA
AACTGGGCCCTGAAGCAGCCACATAAGGTTGTTCCCTTGAAAGGCCTGTGGGAGGAGGAG
GCACCTACACTGCCTGATGGTCACTTTGATGGGATTCTATACGACACATATCCACTGTCT
GAAGAGACCTGGCACACTCACCAGTTCAACTTTATTAAGACTCATGCTTTCCGTTTGCTG
AAGCCTGGGGGTATCCTCACTTACTGCAACCTCACGTCCTGGGGGGAACTCATGAAGTCC
AAGTACACAGACATCACTGCCATGTTTGAGGAGACTCAGGTGCCTGCACTGCTGGAAGCT
GGCTTCCAGAGAGAAAACATCTGTACAGAGGTGATGGCGCTGGTGCCCCCAGCCGACTGC
CGCTACTATGCCTTCCCTCAGATGATCACACCCCTGGTCACCAAGCACTGA
Target 7 GenBank Gene ID
Target 7 GeneCard ID Not Available
Target 7 GenAtlas ID Not Available
Target 7 HGNC ID Not Available
Target 7 Chromosome Location Not Available
Target 7 Locus Not Available
Target 7 SNPs SNPJam Report Link Image
Target 7 General References
  1. Komoto J, Huang Y, Takata Y, Yamada T, Konishi K, Ogawa H, Gomi T, Fujioka M, Takusagawa F: Crystal structure of guanidinoacetate methyltransferase from rat liver: a model structure of protein arginine methyltransferase. J Mol Biol. 2002 Jul 5;320(2):223-35. [PubMed Link Image]
  2. Komoto J, Takata Y, Yamada T, Konishi K, Ogawa H, Gomi T, Fujioka M, Takusagawa F: Monoclinic guanidinoacetate methyltransferase and gadolinium ion-binding characteristics. Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1589-96. Epub 2003 Aug 19. [PubMed Link Image]
  3. Fujioka M, Takata Y, Gomi T: Recombinant rat guanidinoacetate methyltransferase: structure and function of the NH2-terminal region as deduced by limited proteolysis. Arch Biochem Biophys. 1991 Feb 15;285(1):181-6. [PubMed Link Image]
  4. Ogawa H, Date T, Gomi T, Konishi K, Pitot HC, Cantoni GL, Fujioka M: Molecular cloning, sequence analysis, and expression in Escherichia coli of the cDNA for guanidinoacetate methyltransferase from rat liver. Proc Natl Acad Sci U S A. 1988 Feb;85(3):694-8. [PubMed Link Image]
  5. Ogawa H, Fujioka M: Nucleotide sequence of the rat guanidinoacetate methyltransferase gene. Nucleic Acids Res. 1988 Sep 12;16(17):8715-6. [PubMed Link Image]
Target 7 Drug References
  1. Komoto J, Yamada T, Takata Y, Konishi K, Ogawa H, Gomi T, Fujioka M, Takusagawa F: Catalytic mechanism of guanidinoacetate methyltransferase: crystal structures of guanidinoacetate methyltransferase ternary complexes. Biochemistry. 2004 Nov 16;43(45):14385-94. [PubMed Link Image]
  2. 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]
  3. 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]
  4. Karelin AA, Mardashev SR: [The stimulating effect of cyclic AMP, glucagon and insulin on guanidine acetate-N-methyltransferase activity in rat liver and pancreas] Biokhimiia. 1976 Feb;41(2):316-23. [PubMed Link Image]
Drug Target 8 [top]
Target 8 ID 4342
Target 8 Name Divalent-cation tolerance protein cutA
Target 8 Synonyms Not Available
Target 8 Gene Name cutA
Target 8 Protein Sequence >Divalent-cation tolerance protein cutA 
MIIVYTTFPDWESAEKVVKTLLKERLIACANLREHRAFYWWEGKIEEDKEVGAILKTRED
LWEELKERIKELHPYDVPAIIRIDVDDVNEDYLKWLIEETKK
Target 8 Number of Residues 103
Target 8 Molecular Weight 12348
Target 8 Theoretical pI 4.63
Target 8 GO Classification Not Available
Target 8 General Function Inorganic ion transport and metabolism
Target 8 Specific Function Involved in resistance toward heavy metals
Target 8 Pathways Not Available
Target 8 Reactions Not Available
Target 8 Pfam Domain Function
Target 8 Signals
  • None
Target 8 Transmembrane Regions
  • None
Target 8 Essentiality Essential
Target 8 GenBank ID Protein Not Available
Target 8 UniProtKB/Swiss-Prot ID O58720 Link Image
Target 8 UniProtKB/Swiss-Prot Entry Name CUTA_PYRHO Link Image
Target 8 PDB ID 1UKU Link Image
Target 8 PDB File Show
Target 8 3D Structure
Target 8 Cellular Location
  • Cytoplasm
Target 8 Gene Sequence >309 bp 
ATGATAATAGTTTACACGACTTTTCCGGACTGGGAGAGTGCTGAGAAAGTTGTGAAAACT
CTTTTAAAAGAGAGGTTGATTGCATGCGCAAATTTAAGGGAGCACAGGGCCTTTTACTGG
TGGGAAGGTAAGATCGAGGAAGATAAAGAAGTTGGAGCTATCCTTAAAACTAGGGAAGAT
CTGTGGGAAGAACTTAAGGAAAGGATAAAGGAGCTTCATCCTTACGATGTTCCGGCCATA
ATCAGGATTGACGTTGATGATGTTAACGAGGATTACCTCAAATGGTTAATTGAAGAGACG
AAAAAATGA
Target 8 GenBank Gene ID
Target 8 GeneCard ID Not Available
Target 8 GenAtlas ID Not Available
Target 8 HGNC ID Not Available
Target 8 Chromosome Location Not Available
Target 8 Locus Not Available
Target 8 SNPs SNPJam Report Link Image
Target 8 General References
  1. Kawarabayasi Y, Sawada M, Horikawa H, Haikawa Y, Hino Y, Yamamoto S, Sekine M, Baba S, Kosugi H, Hosoyama A, Nagai Y, Sakai M, Ogura K, Otsuka R, Nakazawa H, Takamiya M, Ohfuku Y, Funahashi T, Tanaka T, Kudoh Y, Yamazaki J, Kushida N, Oguchi A, Aoki K, Kikuchi H: Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3. DNA Res. 1998 Apr 30;5(2):55-76. [PubMed Link Image]
Target 8 Drug References Not Available
Drug Target 9 [top]
Target 9 ID 5126
Target 9 Name Arginase
Target 9 Synonyms
  1. EC 3.5.3.1
Target 9 Gene Name rocF
Target 9 Protein Sequence >Arginase 
MKPISIIGVPMDLGQTRRGVDMGPSAMRYAGVIERLERLHYDIEDLGDIPIGKAERLHEQ
GDSRLRNLKAVAEANEKLAAAVDQVVQRGRFPLVLGGDHSIAIGTLAGVAKHYERLGVIW
YDAHGDVNTAETSPSGNIHGMPLAASLGFGHPALTQIGGYSPKIKPEHVVLIGVRSLDEG
EKKFIREKGIKIYTMHEVDRLGMTRVMEETIAYLKERTDGVHLSLDLDGLDPSDAPGVGT
PVIGGLTYRESHLAMEMLAEAQIITSAEFVEVNPILDERNKTASVAVALMGSLFGEKLM
Target 9 Number of Residues 303
Target 9 Molecular Weight 32434
Target 9 Theoretical pI 5.77
Target 9 GO Classification
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
arginase activity
Process
physiological process
metabolism
urea cycle intermediate metabolism
arginine metabolism
arginine catabolism
Component
Not Available
Target 9 General Function Involved in arginase activity
Target 9 Specific Function Controls arginine catabolism
Target 9 Pathways Not Available
Target 9 Reactions Not Available
Target 9 Pfam Domain Function
Target 9 Signals
  • None
Target 9 Transmembrane Regions
  • None
Target 9 Essentiality Essential
Target 9 GenBank ID Protein Not Available
Target 9 UniProtKB/Swiss-Prot ID P53608 Link Image
Target 9 UniProtKB/Swiss-Prot Entry Name ARGI_BACCD Link Image
Target 9 PDB ID 5CEV Link Image
Target 9 PDB File Show
Target 9 3D Structure
Target 9 Cellular Location
  • Cytoplasmic
Target 9 Gene Sequence >900 bp 
ATGAAGCCAATTTCAATTATCGGGGTTCCGATGGATTTAGGGCAGACACGCCGCGGCGTT
GATATGGGGCCGAGCGCAATGCGTTATGCAGGCGTCATCGAACGTCTGGAACGTCTTCAT
TACGATATTGAAGATTTGGGAGATATTCCGATTGGAAAAGCAGAGCGGTTGCACGAGCAA
GGAGATTCACGGTTGCGCAATTTGAAAGCGGTTGCGGAAGCGAACGAGAAACTTGCGGCG
GCGGTTGACCAAGTCGTTCAGCGGGGGCGATTTCCGCTTGTGTTGGGCGGCGACCATAGC
ATCGCCATTGGCACGCTCGCCGGGGTGGCGAAACATTATGAGCGGCTTGGAGTGATCTGG
TATGACGCGCATGGCGACGTCAACACCGCGGAAACGTCGCCGTCTGGAAACATTCATGGC
ATGCCGCTGGCGGCGAGCCTCGGGTTTGGCCATCCGGCGCTGACGCAAATCGGCGGATAC
AGCCCCAAAATCAAGCCGGAACATGTCGTGTTGATCGGCGTCCGTTCCCTTGATGAAGGG
GAGAAGAAGTTTATTCGCGAAAAAGGAATCAAAATTTACACGATGCATGAGGTTGATCGG
CTCGGAATGACAAGGGTGATGGAAGAAACGATCGCCTATTTAAAAGAACGAACGGATGGC
GTTCATTTGTCGCTTGACTTGGATGGCCTTGACCCAAGCGACGCACCGGGAGTCGGAACG
CCTGTCATTGGAGGATTGACATACCGCGAAAGCCATTTGGCGATGGAGATGCTGGCCGAG
GCACAAATCATCACTTCAGCGGAATTTGTCGAAGTGAACCCGATCTTGGATGAGCGGAAC
AAAACAGCATCAGTGGCTGTAGCGCTGATGGGGTCGTTGTTTGGTGAAAAACTCATGTAA
Target 9 GenBank Gene ID
Target 9 GeneCard ID Not Available
Target 9 GenAtlas ID Not Available
Target 9 HGNC ID Not Available
Target 9 Chromosome Location Not Available
Target 9 Locus Not Available
Target 9 SNPs SNPJam Report Link Image
Target 9 General References
  1. Bewley MC, Jeffrey PD, Patchett ML, Kanyo ZF, Baker EN: Crystal structures of Bacillus caldovelox arginase in complex with substrate and inhibitors reveal new insights into activation, inhibition and catalysis in the arginase superfamily. Structure. 1999 Apr 15;7(4):435-48. [PubMed Link Image]
  2. Bewley MC, Lott JS, Baker EN, Patchett ML: The cloning, expression and crystallisation of a thermostable arginase. FEBS Lett. 1996 May 20;386(2-3):215-8. [PubMed Link Image]
Target 9 Drug References Not Available

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.