Biology:X-methyl-His dipeptidase
From HandWiki
| Xaa-methyl-His dipeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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
- ↑ "The free amino acids of fish; 1-methylhistidine and beta-alanine liberation by skeletal muscle anserinase of codling (Gadus callarias)". The Biochemical Journal 60 (1): 81–7. May 1955. PMID 14363188.
- ↑ "Alpha-N-acetyl-L-histidine amidohydrolase activity from the brain of the skipjack tuna Katsuwonus pelamis". Canadian Journal of Biochemistry 45 (2): 337–40. February 1967. doi:10.1139/o67-037. PMID 6067033.
- ↑ "Similarity of tuna N-acetylhistidine deacetylase and cod fish anserinase". Comparative Biochemistry and Physiology. B, Comparative Biochemistry 61 (2): 253–8. 1978. 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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