| EC |
6.3.2.11 |
| Accepted name: |
carnosine synthase |
| Reaction: |
ATP + L-histidine + β-alanine = ADP + phosphate + carnosine |
| Glossary: |
carnosine = N-β-alanyl-L-histidine |
| Other name(s): |
carnosine synthetase; carnosine-anserine synthetase; homocarnosine-carnosine synthetase; carnosine-homocarnosine synthetase; L-histidine:β-alanine ligase (AMP-forming) (incorrect) |
| Systematic name: |
L-histidine:β-alanine ligase (ADP-forming) |
| Comments: |
This enzyme was thought to form AMP [1,2], but studies with highly purified enzyme proved that it forms ADP [4]. Carnosine is a dipeptide that is present at high concentrations in skeletal muscle and the olfactory bulb of vertebrates [3]. It is also found in the skeletal muscle of some invertebrates. The enzyme can also catalyse the formation of homocarnosine from 4-aminobutanoate and L-histidine, with much lower activity [4]. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 9023-61-4 |
| References: |
| 1. |
Kalyankar, G.D. and Meister, A. Enzymatic synthesis of carnosine and related β-alanyl and γ-aminobutyryl peptides. J. Biol. Chem. 234 (1959) 3210–3218. [PMID: 14404206] |
| 2. |
Stenesh, J.J. and Winnick, T. Carnosine-anserine synthetase of muscle. 4. Partial purification of the enzyme and further studies of β-alanyl peptide synthesis. Biochem. J. 77 (1960) 575–581. [PMID: 16748858] |
| 3. |
Crush, K.G. Carnosine and related substances in animal tissues. Comp. Biochem. Physiol. 34 (1970) 3–30. [PMID: 4988625] |
| 4. |
Drozak, J., Veiga-da-Cunha, M., Vertommen, D., Stroobant, V. and Van Schaftingen, E. Molecular identification of carnosine synthase as ATP-grasp domain-containing protein 1 (ATPGD1). J. Biol. Chem. 285 (2010) 9346–9356. [DOI] [PMID: 20097752] |
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| [EC 6.3.2.11 created 1965, modified 2010] |
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