期刊
COMPTES RENDUS BIOLOGIES
卷 328, 期 6, 页码 568-575出版社
EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.crvi.2005.03.005
关键词
lac operon; galactoside; acetyltransferase; acyltransferase; CoenzymeA; LacA
类别
资金
- NIAID NIH HHS [AI-42154] Funding Source: Medline
Of the proteins encoded by the three structural genes of the lac operon, the galactoside acetyltransferase (thiogalactoside transacetylase, LacA, GAT) encoded by lacA is the only protein whose biological role remains in doubt. Here, we briefly note the classical literature that led to the identification and initial characterization of GAT, and focus oil more recent results which have revealed its chemical mechanism of action and its membership in a large superfamily of structurally similar acyltransferases. The structural and sequence similarities of several members of this superfamily confirm the original claim for GAT as a CoA-dependent acetyltransferase specific for the 6-hydroxyl group of certain pyranosides, but do not yet point to the identity of the natural substrate(s) of the enzyme. (c) 2005 Academie des sciences. Published by Elsevier SAS. All rights reserved.
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