Carnosine synthase
Class of enzymes / From Wikipedia, the free encyclopedia
Carnosine synthase (EC 6.3.2.11) is an enzyme that catalyzes the chemical reaction
- ATP + L-histidine + beta-alanine ADP + phosphate + carnosine
Quick Facts Identifiers, EC no. ...
carnosine synthase | |||||||||
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Identifiers | |||||||||
EC no. | 6.3.2.11 | ||||||||
CAS no. | 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 / QuickGO | ||||||||
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The 3 substrates of this enzyme are ATP, L-histidine, and beta-alanine, whereas its 3 products are ADP (previously thought to form AMP[1]), 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)' (incorrect on AMP-forming[2]). Other names in common use include 'carnosine synthetase', 'carnosine-anserine synthetase', 'homocarnosine synthetase', and 'carnosine-homocarnosine synthetase'.