X-methyl-His dipeptidase
Xaa-methyl-His dipeptidase | |||||||||
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Identifiers | |||||||||
EC number | 3.4.13.5 | ||||||||
CAS number | 9027-38-7 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Xaa-methyl-His dipeptidase (EC 3.4.13.5, anserinase, aminoacyl-methylhistidine dipeptidase, acetylhistidine deacetylase, N-acetylhistidine deacetylase, alpha-N-acetyl-L-histidine aminohydrolase) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Hydrolysis of anserine (beta-alanyl!Npi-methyl-L-histidine), carnosine, homocarnosine, glycyl!leucine and other dipeptides with broad specificity
References
- ↑ Jones, N.R. (1955). "The free amino acids of fish. 1-Methylhistidine and β-alanine liberation by skeletal muscle anserinase of codling (Gadus callarias)". Biochem. J. 60: 81–87. PMID 14363188.
- ↑ Baslow, M.H.; Lenney, J.F. (1967). "α-N-Acetyl-L-histidine amidohydrolase activity from the brain of the skipjack tuna Katsuwonus pelamis". Can. J. Biochem. 45: 337–340. doi:10.1139/o67-037. PMID 6067033.
- ↑ Lenney, J.F.; Baslow, M.H.; Sugiyama, G.H. (1978). "Similarity of tuna N-acetylhistidine deacetylase and cod fish anserinase". Comp. Biochem. Physiol. B Comp. Biochem. 61: 253–258. doi:10.1016/0305-0491(78)90171-2. PMID 318374.
External links
- Xaa-methyl-His dipeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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