Carnosine synthase
| carnosine synthase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 6.3.2.11 | ||||||
| CAS number | 9023-61-4 | ||||||
| Databases | |||||||
| IntEnz | IntEnz view | ||||||
| BRENDA | BRENDA entry | ||||||
| ExPASy | NiceZyme view | ||||||
| KEGG | KEGG entry | ||||||
| MetaCyc | metabolic pathway | ||||||
| PRIAM | profile | ||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||
| Gene Ontology | AmiGO / EGO | ||||||
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In enzymology, a carnosine synthase (EC 6.3.2.11) is an enzyme that catalyzes the chemical reaction
- ATP + L-histidine + beta-alanine
AMP + diphosphate + carnosine
The 3 substrates of this enzyme are ATP, L-histidine, and beta-alanine, whereas its 3 products are AMP, diphosphate, and carnosine.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is L-histidine:beta-alanine ligase (AMP-forming). Other names in common use include carnosine synthetase, carnosine-anserine synthetase, homocarnosine-carnosine synthetase, and carnosine-homocarnosine synthetase. This enzyme participates in 4 metabolic pathways: urea cycle and metabolism of amino groups, alanine and aspartate metabolism, histidine metabolism, and beta-alanine metabolism.
References
- KALYANKAR GD, MEISTER A (1959). "Enzymatic synthesis of carnosine and related beta-alanyl and gamma-aminobutyryl peptides". J. Biol. Chem. 234: 3210–8. PMID 14404206.
- Stenesh JJ and Winnick T (1960). "Carnosine–anserine synthetase of muscle. 4. Partial purification of the enzyme and further studies of β-alanyl peptide synthesis". Biochem. J. 77 (3): 575–581. PMC 1205078. PMID 16748858. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1205078.