| EC |
2.3.1.79 |
| Accepted name: |
maltose O-acetyltransferase |
| Reaction: |
acetyl-CoA + maltose = CoA + 6-O-acetyl-α-D-glucopyranosyl-(1→4)-D-glucose |
| Other name(s): |
maltose transacetylase; maltose O-acetyltransferase; MAT |
| Systematic name: |
acetyl-CoA:maltose O-acetyltransferase |
| Comments: |
Not identical with EC 2.3.1.18, galactoside O-acetyltransferase. The acetyl group is added exclusively to the C6 position of glucose and to the C6 position of the non-reducing glucose residue of maltose [3]. Other substrates of this enzyme are glucose, which is a better substrate than maltose [2], and mannose and frucose, which are poorer substrates than maltose [2]. Isopropyl-β-thio-galactose, which is a good substrate for EC 2.3.1.118 is a poor substrate for this enzyme [3]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 81295-47-8 |
| References: |
| 1. |
Freundlieb, S. and Boos, W. Maltose transacetylase of Escherichia coli: a preliminary report. Ann. Microbiol. (Paris) 133A (1982) 181–189. [PMID: 7041741] |
| 2. |
Brand, B. and Boos, W. Maltose transacetylase of Escherichia coli. Mapping and cloning of its structural, gene, mac, and characterization of the enzyme as a dimer of identical polypeptides with a molecular weight of 20,000. J. Biol. Chem. 266 (1991) 14113–14118. [PMID: 1856235] |
| 3. |
Lo Leggio, L., Dal Degan, F., Poulsen, P., Andersen, S.M. and Larsen, S. The structure and specificity of Escherichia coli maltose
acetyltransferase give new insight into the LacA family of
acyltransferases. Biochemistry 42 (2003) 5225–5235. [DOI] [PMID: 12731863] |
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| [EC 2.3.1.79 created 1984] |
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