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A novel esterase subfamily with α/β‐hydrolase fold suggested by structures of two bacterial enzymes homologous to l ‐homoserine O ‐acetyl transferases
Author(s) -
Tölzer Christine,
Pal Sonia,
Watzlawick Hildegard,
Altenbuchner Josef,
Niefind Karsten
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12031
Subject(s) - esterase , subfamily , hydrolase , homoserine , biochemistry , enzyme , uniprot , protein superfamily , biology , chemistry , gene , quorum sensing , virulence
MekB from Pseudomonas veronii and Cg Hle from Corynebacteriumglutamicum belong to the superfamily of α/β‐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 Cg Hle 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 Cg Hle to bind homoserine and acetyl‐CoA. Insofar the MekB and Cg Hle structures suggest dividing the homoserine transacetylase family into subfamilies, namely genuine acetyl transferases and acetyl esterases with MekB and Cg Hle as constituting members of the latter.