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discounted EARLY registration ends Dec 31, 2014
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Escherichia coli K-12 substr. MG1655 Reaction: 2.3.1.79

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 2.3.1.79

Enzymes and Genes:
maltose acetyltransferase Inferred from experiment : maa

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name: maltose O-acetyltransferase

Enzyme Commission Synonyms: maltose transacetylase, maltose O-acetyltransferase, MAT

Summary:
This reaction acetylates free sugars in the cell, perhaps playing a detoxifying role.

Enzyme Commission Summary:
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 [Lo03a]. Other substrates of this enzyme are glucose, which is a better substrate than maltose [Brand91], and mannose and frucose, which are poorer substrates than maltose [Brand91]. Isopropyl-β-thio-galactose, which is a good substrate for EC 2.3.1.118 is a poor substrate for this enzyme [Lo03a].

Citations: [Freundlieb82]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:2.3.1.79 , ENZYME:EC:2.3.1.79 , IUBMB-ExplorEnz:EC:2.3.1.79


References

Brand91: 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 1991;266(21);14113-8. PMID: 1856235

Freundlieb82: Freundlieb S, Boos W (1982). "Maltose transacetylase of Escherichia coli: a preliminary report." Ann Microbiol (Paris) 1982;133A(1);181-9. PMID: 7041741

Lo03a: 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. PMID: 12731863


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sun Dec 21, 2014, BIOCYC14B.