In enzymology, a maltose O-acetyltransferase (EC 2.3.1.79) is an enzyme that catalyzes the chemical reaction
maltose O-acetyltransferase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 2.3.1.79 | ||||||||
CAS no. | 81295-47-8 | ||||||||
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 | ||||||||
|
- acetyl-CoA + maltose CoA + 6-O-acetyl-alpha-D-glucopyranosyl-(1->4)-D-glucose
Thus, the two substrates of this enzyme are acetyl-CoA and maltose, whereas its two products are CoA and [[6-O-acetyl-alpha-D-glucopyranosyl-(1->4)-D-glucose]].
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:maltose O-acetyltransferase. Other names in common use include maltose transacetylase, maltose O-acetyltransferase, and MAT.
Structural studies
editAs of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1OCX, 2IC7, and 2P2O.
References
edit- Freundlieb S, Boos W (January 1982). "Maltose transacetylase of Escherichia coli: a preliminary report". Ann. Microbiol. 133A (1). Paris: 181–9. PMID 7041741.
- Brand B, Boos W (1991). "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 (21): 14113–8. doi:10.1016/S0021-9258(18)92816-4. PMID 1856235.
- Lo Leggio L, Dal Degan F, Poulsen P, Andersen SM, Larsen S (2003). "The structure and specificity of Escherichia coli maltose acetyltransferase give new insight into the LacA family of acyltransferases". Biochemistry. 42 (18): 5225–35. doi:10.1021/bi0271446. PMID 12731863.