Tolzer C

References (2)

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_2016_FEBS.Lett_590_174
Author(s) : Tolzer C , Pal S , Watzlawick H , Altenbuchner J , Niefind K
Ref : FEBS Letters , 590 :174 , 2016
Abstract : 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.
ESTHER : Tolzer_2016_FEBS.Lett_590_174
PubMedSearch : Tolzer_2016_FEBS.Lett_590_174
PubMedID: 26787467
Gene_locus related to this paper: 9psed-q0mrg5

Title : Crystallization and preliminary crystallographic analysis of cgHle, a homoserine acetyltransferase homologue, from Corynebacterium glutamicum - Tolzer_2009_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_65_34
Author(s) : Tolzer C , Pal S , Watzlawick H , Altenbuchner J , Niefind K
Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 65 :34 , 2009
Abstract : CgHle is an enzyme that is encoded by gene cg0961 from Corynebacterium glutamicum. The physiological function of cgHle is so far unclear. Bioinformatic annotations based on sequence homology indicated that cgHle may be an acetyl-CoA:homoserine acetyl transferase and as such may be involved in methionine biosynthesis, but recent evidence has shown that it is an esterase that catalyzes the hydrolysis of acetyl esters. Here, the crystallization of cgHle in two orthorhombic crystal forms, a trigonal crystal form and a monoclinic crystal form is described. The trigonal crystals have a solvent content of 83.7%, which is one of the highest solvent contents ever found for protein crystals. One of the orthorhombic crystals diffracted X-rays to at least 1.2 A resolution.
ESTHER : Tolzer_2009_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_65_34
PubMedSearch : Tolzer_2009_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_65_34
PubMedID: 19153452
Gene_locus related to this paper: corgl-CGL0839