Carnosine synthase

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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 $\rightleftharpoons$ 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.

[edit] References

IUBMB entry for 6.3.2.11
BRENDA references for 6.3.2.11 (Recommended.)
PubMed references for 6.3.2.11
PubMed Central references for 6.3.2.11
Google Scholar references for 6.3.2.11
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 beta-alanyl peptide synthesis". Biochem. J. 77: 575–581.