Toelzer et al. showed that MekB (9psed-q0mrg5) from Pseudomonas veronii and CgHle (corgl-CGL0839) from Corynebacteriumglutamicum are esterases that hydrolyse preferentially acetic acid esters. MekB and CgHle cannot bind homoserine and acetyl-CoA. Accordingly a novel esterase subfamily was extracted from the Homoserine_transacetylase family
Title: A novel esterase subfamily with alpha/beta-hydrolase fold suggested by structures of two bacterial enzymes homologous to l-homoserine O-acetyl transferases Tolzer C, Pal S, Watzlawick H, Altenbuchner J, Niefind K Ref: FEBS Letters, 590:174, 2016 : PubMed
MekB from Pseudomonas veronii and CgHle from Corynebacteriumglutamicum belong to the superfamily of alpha/beta-hydrolase fold proteins. Based on sequence comparisons, they are annotated as homoserine transacetylases in popular databases like UNIPROT, PFAM or ESTHER. However, experimentally, MekB and CgHle were shown to be esterases that hydrolyse preferentially acetic acid esters. We describe the x-ray structures of these enzymes solved to high resolution. The overall structures confirm the close relatedness to experimentally validated homoserine acetyl transferases, but simultaneously the structures exclude the ability of MekB and CgHle to bind homoserine and acetyl-CoA. Insofar the MekB and CgHle structures suggest dividing the homoserine transacetylase family into subfamilies, namely genuine acetyl transferases and acetyl esterases with MekB and CgHle as constituting members of the latter.
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No structure scheme yet for this family
Structures in Homoserine_transacetylase_like_est family (4)
