Universität zu Köln

Toelzer, Christine ORCID: 0000-0001-9984-5940, Pal, Sonia, Watzlawick, Hildegard, Altenbuchner, Josef and Niefind, Karsten ORCID: 0000-0002-0183-6315 (2016). A novel esterase subfamily with alpha/beta-hydrolase fold suggested by structures of two bacterial enzymes homologous to L-homoserine O-acetyl transferases. FEBS Lett., 590 (1). S. 174 - 185. HOBOKEN: WILEY. ISSN 1873-3468

Full text not available from this repository.

Abstract

MekB from Pseudomonas veronii and CgHle from Corynebacteriumglutamicum belong to the superfamily of /-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.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Toelzer, Christine UNSPECIFIED orcid.org/0000-0001-9984-5940 UNSPECIFIED Pal, Sonia UNSPECIFIED UNSPECIFIED UNSPECIFIED Watzlawick, Hildegard UNSPECIFIED UNSPECIFIED UNSPECIFIED Altenbuchner, Josef UNSPECIFIED UNSPECIFIED UNSPECIFIED Niefind, Karsten UNSPECIFIED orcid.org/0000-0002-0183-6315 UNSPECIFIED
URN:	urn:nbn:de:hbz:38-291489
DOI:	10.1002/1873-3468.12031
Journal or Publication Title:	FEBS Lett.
Volume:	590
Number:	1
Page Range:	S. 174 - 185
Date:	2016
Publisher:	WILEY
Place of Publication:	HOBOKEN
ISSN:	1873-3468
Language:	English
Faculty:	Faculty of Mathematics and Natural Sciences
Divisions:	Faculty of Mathematics and Natural Sciences > Department of Chemistry > Institute of Biochemistry
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language CRYSTAL-STRUCTURE; ACETYLTRANSFERASE; TRANSACETYLASE; PROMISCUITY; SUPERFAMILY; DATABASE; TARGET; TOOLS Multiple languages Biochemistry & Molecular Biology; Biophysics; Cell Biology Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/29148