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Human Metabolome Database Version 2.5

 

Showing metabocard for Cysteamine (HMDB02991)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-05-22 16:12:24
Update Date 2010-04-18 16:38:51
Accession Number HMDB02991
Secondary Accession Numbers Not Available
Common Name Cysteamine
Description Cysteamine is a product of the constitutive degradation of coenzyme A, a process that occurs in all tissues, although some tissues such as brain and heart may have exceptionally high coenzyme A turnover rates. Cysteamine has only one known function, and that is as a precursor for the formation of hypotaurine, which is subsequently oxidized to taurine. The rate of cysteamine production as a result of coenzyme A breakdown is not well understood but it is clear that cysteamine levels are not as dramatically affected by dietary habits as are cysteine levels. Cysteamine is generated from hypotaurine by cysteamine dioxygenase (EC:1.13.11.19), an enzyme that was recently identified in mammals (PMID: 17581819). Cysteamine is the simplest stable aminothiol found in the body. It is used in the treatment of disorders of cystine excretion. Cysteamine cleaves the disulfide bond with cysteine to produce molecules that can escape the metabolic defect in cystinosis and cystinuria. Cyst(e)amine may also serve as an endogenous regulator of immune system activity as well as a potential therapeutic agent for the treatment of Huntington disease. Cysteamine is also used as a radiation-protective agent that oxidizes in air to form cystamine. It can be given intravenously or orally to treat radiation sickness. -- Wikipedia
Synonyms
  1. (2-Mercaptoethyl)amine
  2. 2-Amino-1-ethanethiol
  3. 2-Aminoethanethiol
  4. 2-Aminoethyl mercaptan
  5. 2-Mercaptoethanamine
  6. Aminoethyl mercaptan
  7. Becaptan
  8. Cisteamina
  9. Cysteamide
  10. Cysteamin
  11. Cysteamine
  12. Cysteinamine
  13. Decarboxycysteine
  14. Ethanethiolamine
  15. Lambraten
  16. Lambratene
  17. Mecramine
  18. Mercamin
  19. Mercamine
  20. Mercaptamin
  21. Merkamin
  22. Riacon
  23. Thioethanolamine
  24. b-Aminoethanethiol
  25. b-Aminoethylthiol
  26. b-Mercaptoethylamine
  27. beta-Aminoethanethiol
  28. beta-Mercaptoethylamine
  29. beta-Aminoethylthiol
  30. CASH
Chemical IUPAC Name 2-aminoethanethiol
Chemical Formula C2H7NS
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amines
Class
  • Aliphatic and Aryl Amines
Sub Class
  • Tertiary aliphatic amines
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aliphatic amine (alkylamine)
  • thiol (sulfanyl compound)
  • alkylthiol
Biofunction
  • Redox control, taurine synthesis and sulfur metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 77.149
Monoisotopic Molecular Weight 77.029922
Isomeric SMILES NCCS
Canonical SMILES NCCS
KEGG Compound ID C01678 Link Image
BioCyc ID CPD-3721 Link Image
BiGG ID 1808054 Link Image
Wikipedia Link Cysteamine Link Image
NuGOwiki Link HMDB02991 Link Image
Metagene Link HMDB02991 Link Image
METLIN ID 3222 Link Image
PubChem Compound 6058 Link Image
PubChem Substance 11369773 Link Image
ChEBI ID 17141 Link Image
CAS Registry Number 60-23-1
InChI Identifier InChI=1/C2H7NS/c3-1-2-4/h4H,1-3H2
Synthesis Reference Not Available
Melting Point (Experimental) 98 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 486 mg/mL at 25 oC [MEYLAN,WM et al. (1996)]; 23.5 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 0.01 [Predicted by ALOGPS]; 0.1 [Predicted by PubChem via XLOGP]; -0.20 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
Biofluid Location Not Available
Tissue Location
Tissue References
Leukocyte —
Muscle —
Pancreas —
Spleen —
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Taurine and Hypotaurine Metabolism SMP00021 Link Image map00430 Link Image
General References
  1. Chakrabarti MC, Le N, Paik CH, De Graff WG, Carrasquillo JA: Prevention of radiolysis of monoclonal antibody during labeling. J Nucl Med. 1996 Aug;37(8):1384-8. [PubMed Link Image]
  2. Skov Olsen P: Role of epidermal growth factor in gastroduodenal mucosal protection. J Clin Gastroenterol. 1988;10 Suppl 1:S146-51. [PubMed Link Image]
  3. Gahl WA, Schneider JA, Schulman JD, Thoene JG, Reed GF: Predicted reciprocal serum creatinine at age 10 years as a measure of renal function in children with nephropathic cystinosis treated with oral cysteamine. Pediatr Nephrol. 1990 Mar;4(2):129-35. [PubMed Link Image]
  4. Smolin LA, Clark KF, Thoene JG, Gahl WA, Schneider JA: A comparison of the effectiveness of cysteamine and phosphocysteamine in elevating plasma cysteamine concentration and decreasing leukocyte free cystine in nephropathic cystinosis. Pediatr Res. 1988 Jun;23(6):616-20. [PubMed Link Image]
  5. Levtchenko EN, van Dael CM, de Graaf-Hess AC, Wilmer MJ, van den Heuvel LP, Monnens LA, Blom HJ: Strict cysteamine dose regimen is required to prevent nocturnal cystine accumulation in cystinosis. Pediatr Nephrol. 2006 Jan;21(1):110-3. Epub 2005 Oct 27. [PubMed Link Image]
  6. Lochman P, Adam T, Friedecky D, Hlidkova E, Skopkova Z: High-throughput capillary electrophoretic method for determination of total aminothiols in plasma and urine. Electrophoresis. 2003 Apr;24(7-8):1200-7. [PubMed Link Image]
  7. Sonies BC, Almajid P, Kleta R, Bernardini I, Gahl WA: Swallowing dysfunction in 101 patients with nephropathic cystinosis: benefit of long-term cysteamine therapy. Medicine (Baltimore). 2005 May;84(3):137-46. [PubMed Link Image]
  8. Liu YC, Wang CM, Hsiung KP: Comparison of different protein immobilization methods on quartz crystal microbalance surface in flow injection immunoassay. Anal Biochem. 2001 Dec 15;299(2):130-5. [PubMed Link Image]
  9. Yudkoff M, Foreman JW, Segal S: Effects of cysteamine therapy in nephropathic cystinosis. N Engl J Med. 1981 Jan 15;304(3):141-5. [PubMed Link Image]
  10. Gahl WA, Charnas L, Markello TC, Bernardini I, Ishak KG, Dalakas MC: Parenchymal organ cystine depletion with long-term cysteamine therapy. Biochem Med Metab Biol. 1992 Dec;48(3):275-85. [PubMed Link Image]
  11. Geelen JM, Monnens LA, Levtchenko EN: Follow-up and treatment of adults with cystinosis in the Netherlands. Nephrol Dial Transplant. 2002 Oct;17(10):1766-70. [PubMed Link Image]
  12. Pastore A, Massoud R, Motti C, Lo Russo A, Fucci G, Cortese C, Federici G: Fully automated assay for total homocysteine, cysteine, cysteinylglycine, glutathione, cysteamine, and 2-mercaptopropionylglycine in plasma and urine. Clin Chem. 1998 Apr;44(4):825-32. [PubMed Link Image]
  13. Stachowicz M, Lehmann B, Tibi A, Prognon P, Daurat V, Pradeau D: Determination of total cysteamine in human serum by a high-performance liquid chromatography with fluorescence detection. J Pharm Biomed Anal. 1998 Aug;17(4-5):767-73. [PubMed Link Image]
  14. Orloff S, Butler JD, Towne D, Mukherjee AB, Schulman JD: Pantetheinase activity and cysteamine content in cystinotic and normal fibroblasts and leukocytes. Pediatr Res. 1981 Jul;15(7):1063-7. [PubMed Link Image]
  15. de Graaf-Hess A, Trijbels F, Blom H: New method for determining cystine in leukocytes and fibroblasts. Clin Chem. 1999 Dec;45(12):2224-8. [PubMed Link Image]
  16. Chmiel J, Kopczynski Z, Rybczynska M: The influence of the known radioprotective compounds on the metabolism of red blood cells. I. Effect of cysteamine on the cellular level of the intermediates and coenzymes. Pol J Pharmacol Pharm. 1976;28(2):113-21. [PubMed Link Image]
  17. Schneider JA, Clark KF, Greene AA, Reisch JS, Markello TC, Gahl WA, Thoene JG, Noonan PK, Berry KA: Recent advances in the treatment of cystinosis. J Inherit Metab Dis. 1995;18(4):387-97. [PubMed Link Image]
  18. Wikipedia Link Image
Metabolic Enzymes
  1. Somatostatin precursor
  2. Pantetheinase precursor
  3. cDNA FLJ77936, highly similar to Homo sapiens VNN1 protein
  4. Chromosome 10 open reading frame 22
  5. 2-aminoethanethiol dioxygenase
Enzyme 1 [top]
Enzyme 1 ID 6979
Enzyme 1 Name Somatostatin precursor
Enzyme 1 Synonyms
  1. Growth hormone release-inhibiting factor[Contains: Somatostatin-28
  2. Somatostatin-14]
Enzyme 1 Gene Name SST
Enzyme 1 Protein Sequence >Somatostatin precursor 
MLSCRLQCALAALSIVLALGCVTGAPSDPRLRQFLQKSLAAAAGKQELAKYFLAELLSEP
NQTENDALEPEDLSQAAEQDEMRLELQRSANSNPAMAPRERKAGCKNFFWKTFTSC
Enzyme 1 Number of Residues 116
Enzyme 1 Molecular Weight 12736
Enzyme 1 Theoretical pI 5.18
Enzyme 1 GO Classification
Function
  • hormone activity
  • receptor binding
  • signal transducer activity
Process
—
Component
  • extracellular region
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Somatostatin inhibits the release of somatotropin
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-24
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 338288 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P61278 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name SMS_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >351 bp 
ATGCTGTCCTGCCGCCTCCAGTGCGCGCTGGCTGCGCTGTCCATCGTCCTGGCCCTGGGC
TGTGTCACCGGCGCTCCCTCGGACCCCAGACTCCGTCAGTTTCTGCAGAAGTCCCTGGCT
GCTGCCGCGGGGAAGCAGGAACTGGCCAAGTACTTCTTGGCAGAGCTGCTGTCTGAACCC
AACCAGACGGAGAATGATGCCCTGGAACCTGAAGATCTGTCCCAGGCTGCTGAGCAGGAT
GAAATGAGGCTTGAGCTGCAGAGATCTGCTAACTCAAACCCGGCTATGGCACCCCGAGAA
CGCAAAGCTGGCTGCAAGAATTTCTTCTGGAAGACTTTCACATCCTGTTAG
Enzyme 1 GenBank Gene ID J00306 Link Image
Enzyme 1 GeneCard ID SST Link Image
Enzyme 1 GenAtlas ID SST Link Image
Enzyme 1 HGNC ID HGNC:11329 Link Image
Enzyme 1 Chromosome Location 3
Enzyme 1 Locus 3q28
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Shen LP, Pictet RL, Rutter WJ: Human somatostatin I: sequence of the cDNA. Proc Natl Acad Sci U S A. 1982 Aug;79(15):4575-9. [PubMed Link Image]
  2. Shen LP, Rutter WJ: Sequence of the human somatostatin I gene. Science. 1984 Apr 13;224(4645):168-71. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 7344
Enzyme 2 Name Pantetheinase precursor
Enzyme 2 Synonyms
  1. Pantetheine hydrolase
  2. Vascular non-inflammatory molecule 1
  3. Vanin-1
  4. Tiff66
Enzyme 2 Gene Name VNN1
Enzyme 2 Protein Sequence >Pantetheinase precursor 
MTTQLPAYVAILLFYVSRASCQDTFTAAVYEHAAILPNATLTPVSREEALALMNRNLDIL
EGAITSAADQGAHIIVTPEDAIYGWNFNRDSLYPYLEDIPDPEVNWIPCNNRNRFGQTPV
QERLSCLAKNNSIYVVANIGDKKPCDTSDPQCPPDGRYQYNTDVVFDSQGKLVARYHKQN
LFMGENQFNVPKEPEIVTFNTTFGSFGIFTCFDILFHDPAVTLVKDFHVDTIVFPTAWMN
VLPHLSAVEFHSAWAMGMRVNFLASNIHYPSKKMTGSGIYAPNSSRAFHYDMKTEEGKLL
LSQLDSHPSHSAVVNWTSYASSIEALSSGNKEFKGTVFFDEFTFVKLTGVAGNYTVCQKD
LCCHLSYKMSENIPNEVYALGAFDGLHTVEGRYYLQICTLLKCKTTNLNTCGDSAETAST
RFEMFSLSGTFGTQYVFPEVLLSENQLAPGEFQVSTDGRLFSLKPTSGPVLTVTLFGRLY
EKDWASNASSGLTAQARIIMLIVIAPIVCSLSW
Enzyme 2 Number of Residues 513
Enzyme 2 Molecular Weight 57012
Enzyme 2 Theoretical pI 5.26
Enzyme 2 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
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Process
  • metabolism
  • nitrogen compound metabolism
  • physiological process
Component
—
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-21
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 4128047 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O95497 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name VNN1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1542 bp 
ATGACTACTCAGTTGCCAGCTTACGTGGCAATTTTGCTTTTCTATGTCTCAAGAGCCAGC
TGCCAGGACACTTTCATTGCAGCTGTTTATGAGCATGCAGCGATATTGCCCAATGCCACC
CTAACACCAGTGTCTCGTGAGGAGGCTTTGGCATTAATGAATCGGAATCTGGACATTTTG
GAAGGAGCGATCACATCAGCAGCAGATCAGGGTGCGCATATTATTGTGACTCCAGAAGAT
GCTATTTATGGCTGGAACTTCAACAGGGACTCTCTCTACCCATATTTGGAGGACATCCCA
GACCCTGAAGTAAACTGGATCCCCTGTAATAATCGTAACAGATTTGGCCAGACCCCAGTA
CAAGAAAGACTCAGCTGCCTGGCCAAGAACAACTCTATCTATGTTGTGGCAAATATTGGG
GACAAGAAGCCATGCGATACCAGTGATCCTCAGTGTCCCCCTGATGGCCGTTACCAATAC
AACACTGATGTGGTATTTGATTCTCAAGGAAAACTGGTGGCACGCTACCATAAGCAAAAC
CTTTTCATGGGTGAAAATCAATTCAATGTACCCAAGGAGCCTGAGATTGTGACTTTCAAT
ACCACCTTTGGAAGTTTTGGCATTTTCACATGCTTTGATATACTCTTCCATGATCCTGCT
GTTACCTTGGTGAAAGATTTCCACGTGGACACCATAGTATTCCCAACAGCTTGGATGAAT
GTTTTGCCACATTTGTCAGCTGTTGAATTCCACTCAGCTTGGGCTATGGGCATGAGGGTC
AATTTCCTTGCATCCAACATACATTACCCCTCAAAGAAAATGACAGGAAGTGGCATCTAT
GCACCCAATTCTTCAAGAGCATTTCATTATGATATGAAGACAGAAGAGGGAAAACTCCTC
CTCTCGCAACTGGATTCCCACCCATCCCATTCTGCAGTGGTGAACTGGACTTCCTATGCC
AGCAGTATAGAAGCGCTCTCATCAGGAAACAAGGAATTTAAAGGCACTGTCTTTTTCGAT
GAATTCACTTTTGTGAAGCTCACAGGAGTTGCAGGAAATTATACAGTTTGTCAGAAAGAT
CTCTGCTGTCATTTAAGCTACAAAATGTCTGAGAACATACCAAATGAAGTGTACGCTCTA
GGGGCATTTGACGGACTGCACACTGTGGAAGGGCGCTATTATCTACAGATTTGTACCCTG
TTGAAATGTAAAACGACTAATTTAAACACTTGCGGTGACTCAGCTGAAACAGCTTCTACC
AGGTTTGAAATGTTCTCCCTCAGTGGCACTTTCGGAACCCAGTATGTCTTTCCTGAGGTG
TTGCTGAGTGAAAATCAGCTTGCACCTGGAGAATTTCAGGTGTCAACTGACGGACGCTTG
TTTAGTCTGAAGCCAACATCCGGACCTGTCTTAACAGTAACTCTGTTTGGGAGGTTGTAT
GAGAAGGACTGGGCATCAAATGCTTCATCAGGCCTCACAGCACAAGCAAGAATAATAATG
CTAATAGTTATAGCACCTATTGTATGCTCATTAAGTTGGTAG
Enzyme 2 GenBank Gene ID AJ132099 Link Image
Enzyme 2 GeneCard ID VNN1 Link Image
Enzyme 2 GenAtlas ID VNN1 Link Image
Enzyme 2 HGNC ID HGNC:12705 Link Image
Enzyme 2 Chromosome Location 6
Enzyme 2 Locus 6q23-q24
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Galland F, Malergue F, Bazin H, Mattei MG, Aurrand-Lions M, Theillet C, Naquet P: Two human genes related to murine vanin-1 are located on the long arm of human chromosome 6. Genomics. 1998 Oct 15;53(2):203-13. [PubMed Link Image]
  2. 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 Link Image]
  3. Maras B, Barra D, Dupre S, Pitari G: Is pantetheinase the actual identity of mouse and human vanin-1 proteins? FEBS Lett. 1999 Nov 19;461(3):149-52. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 13078
Enzyme 3 Name cDNA FLJ77936, highly similar to Homo sapiens VNN1 protein
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name Not Available
Enzyme 3 Protein Sequence >cDNA FLJ77936, highly similar to Homo sapiens VNN1 protein 
MTTQLPAYVAILLFYVSRASCQDTFIAAVYEHAAILPNATLTPVSREEALALMNRNLDIL
EGAITSAADQGAHIIVTPEDAIYGWNFNRDSLYPYLEDIPDPEVNWIPCNNRNRFGQTPV
QERLSCLAKNNSIYVVANIGDKKPCDTSDPQCPPDGRYQYNTDVVFDSQGKLVARYHKQN
LFMGENQFNVPKEPEIVTFNTTFGSFGIFTCFDILFHDPAVTLVKDFHVDTIVFPTAWMN
VLPHLSAVEFHSAWAMGMRVNFLASNIHYPSKKMTGSGIYAPNSSRAFHYDMKTEEGKLL
LSQLDSHPSHSAVVNWTSYASSIEALSSGNKEFKGTVFFDEFTFVKLTGVAGNYTVCQKD
LCCHLSYKMSENIPNEVYALGAFDGLHTVEGRYYLQICTLLKCKTTNLNTCGDSAETAST
RFEMFSLSGTFGTQYVFPEVLLSENQLAPGEFQVSTDGRLFSLKPTSGPVLTVTLFGRLY
EKDWASNASSGLTAQARIIMLIVIAPIVCSLSW
Enzyme 3 Number of Residues 513
Enzyme 3 Molecular Weight 57024
Enzyme 3 Theoretical pI 5.26
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function Not Available
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 158261873 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID A8K310 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name A8K310_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID AK290425 Link Image
Enzyme 3 GeneCard ID A8K310 Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs Not Available
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 13113
Enzyme 4 Name Chromosome 10 open reading frame 22
Enzyme 4 Synonyms
  1. Chromosome 10 open reading frame 22, isoform CRA_a
Enzyme 4 Gene Name C10orf22
Enzyme 4 Protein Sequence >Chromosome 10 open reading frame 22 
MPRDNMASLIQRIARQACLTFRGSGGGRGASDRDAASGPEAPMQPGFPENLSKLKSLLTQ
LRAEDLNIAPRKATLQPLPPNLPPVTYMHIYETDGFSLGVFLLKSGTSIPLHDHPGMHGM
LKVLYGTVRISCMDKLDAGGGQRPRALPPEQQFEPPLQPREREAVRPGVLRSRAEYTEAS
GPCILTPHRDNLHQIDAVEGPAAFLDILAPPYDPDDGRDCHYYRVLEPVRPKEASSSACD
LPREVWLLETPQADDFWCEGEPYPGPKVFP
Enzyme 4 Number of Residues 270
Enzyme 4 Molecular Weight 29751
Enzyme 4 Theoretical pI Not Available
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function Not Available
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID B1AL29 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name B1AL29_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID Not Available
Enzyme 4 GeneCard ID B1AL29 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 14386
Enzyme 5 Name 2-aminoethanethiol dioxygenase
Enzyme 5 Synonyms
  1. Cysteamine dioxygenase
Enzyme 5 Gene Name ADO
Enzyme 5 Protein Sequence >2-aminoethanethiol dioxygenase 
MPRDNMASLIQRIARQACLTFRGSGGGRGASDRDAASGPEAPMQPGFPENLSKLKSLLTQ
LRAEDLNIAPRKATLQPLPPNLPPVTYMHIYETDGFSLGVFLLKSGTSIPLHDHPGMHGM
LKVLYGTVRISCMDKLDAGGGQRPRALPPEQQFEPPLQPREREAVRPGVLRSRAEYTEAS
GPCILTPHRDNLHQIDAVEGPAAFLDILAPPYDPDDGRDCHYYRVLEPVRPKEASSSACD
LPREVWLLETPQADDFWCEGEPYPGPKVFP
Enzyme 5 Number of Residues 270
Enzyme 5 Molecular Weight 29751
Enzyme 5 Theoretical pI 5.91
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function 2-aminoethanethiol + O(2) = hypotaurine
Enzyme 5 Pathways
  • Taurine and Hypotaurine Metabolism (map00430 Link Image)
Enzyme 5 Reactions
  • 2-aminoethanethiol + O2 = hypotaurine [RN:R02467] ALL_REAC R02467
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 66840146 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q96SZ5 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name AEDO_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >813 bp 
ATGCCCCGAGACAACATGGCCTCCTTGATCCAACGGATCGCCCGCCAGGCTTGCCTCACC
TTCCGGGGCAGCTGGGGCGGCCGCGGCGCTTCCGATCGCGACGCGGCTTCTGGCGCGGAG
GCGCCGATGCAGCCGGGCTTCCCCGAGAACCTGAGCAAGCTGAAGAGCCTCCTGACCCAG
CTCCGCGCCGAGGACTTGAACATCGCCCCGCGCAAGGCCACACTGCAGCCGCTGCCGCCC
AACCTGCCGCCAGTCACCTACATGCACATCTACGAGACGGACGGCTTCAGCCTGGGCGTG
TTCCTGCTCAAGAGCGGCACGTCCATCCCGCTGCACGACCACCCGGGCATGCACGGCATG
CTCAAGGTGCTGTACGGCACCGTGCGCATCAGCTGCATGGACAAGCTAGACGCGGGCGGC
GGGCAACGGCCGCGGGCCTTGCCGCCCGAGCAGCAGTTCGAGCCGCCGCTGCAGCCCCGG
GAGCGAGAAGCCGTGCGGCCGGGCGTGCTGCGTTCGCGGGCCGAGTACACCGAGGCCAGC
GGCCCCTGCATCCTCACACCGCACCGGGACAACCTGCACCAGATCGACGCCGTGGAAGGG
CCTGCCGCCTTCCTGGACATCCTGGCCCCGCCCTACGACCCGGACGATGGCCGGGACTGC
CACTATTACCGGGTGCTGGAGCCGGTCAGGCCCAAGGAGGCCTCCAGCTCGGCCTGTGAC
CTGCCTCGAGAGGTGTGGCTCCTGGAGACCCCACAGGCCGATGACTTCTGGTGCGAGGGA
GAACCCTATCCAGGTCCCAAGGTCTTCCCTTGA
Enzyme 5 GenBank Gene ID BC018660 Link Image
Enzyme 5 GeneCard ID Q96SZ5 Link Image
Enzyme 5 GenAtlas ID ADO Link Image
Enzyme 5 HGNC ID HGNC:23506 Link Image
Enzyme 5 Chromosome Location 10
Enzyme 5 Locus 10q21.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available