Functional implications of structural homologies between chloramphenicol acetyltransferase and dihydrolipoamide acetyltransferase

Publisher Website
Google Scholar
Abstract
Comparisons between the amino acid sequences of the dihydrolipoamide acetyltransferase (E2p) of Escherichia coli and several chloramphenicol acetyltransferases (CATs) have revealed some well-aligned homologies which may be indicative of an underlying structural homology between the catalytic (acetyltransferase) domain of E2p and CAT. The region containing the active-site histidine residue of CAT is particularly well-conserved in E2p and this identifies His-602 as a putative active-site residue of the dihydrolipoamide acetyltransferase. A mechanism for the reversible transacetylation of enzymbe-bound 8-acetyldihydrolipoamide and CoA that is analogous to the proposed mechanism for chloramphenicol acetylation, is presented.

This publication has 0 references indexed in Scilit: