Substrate analysis of homoserine acyltransferase from Bacillus cereus

Substrate specificity within the family of enzymes designated as homoserine transsuccinylases is variable, with some organisms utilizing succinyl-CoA and other organisms utilizing acetyl-CoA. In this study it is shown that the enzyme from Bacillus cereus uses acetyl-CoA as its acyl donor, but its ca...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2007-09, Vol.361 (2), p.510-515
Main Authors: Ziegler, Katharine, Yusupov, Muzaffar, Bishop, Barney, Born, Timothy L.
Format: Article
Language:English
Subjects:
Acyltransfer
Bacillus cereus
Bacillus cereus - enzymology
Cloning, Molecular
Diethyl Pyrocarbonate - pharmacology
Enzyme Activation - drug effects
Escherichia coli
Homoserine - chemistry
Homoserine - metabolism
Homoserine O-Succinyltransferase - isolation & purification
Homoserine O-Succinyltransferase - metabolism
Homoserine transacetylase
Homoserine transsuccinylase
Hydrogen-Ion Concentration
Iodoacetamide - pharmacology
Kinetics
Methionine - metabolism
Methionine biosynthesis
Mutant Proteins - metabolism
Nitrophenols - pharmacology
Substrate Specificity - drug effects
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Summary:Substrate specificity within the family of enzymes designated as homoserine transsuccinylases is variable, with some organisms utilizing succinyl-CoA and other organisms utilizing acetyl-CoA. In this study it is shown that the enzyme from Bacillus cereus uses acetyl-CoA as its acyl donor, but its catalytic rate is significantly lower than other HTS family members. BcHTS is inactivated by both iodoacetamide and diethyl pyrocarbonate and the enzyme can be partially protected from inactivation by the presence of succinyl-CoA. This leads to the conclusion that BcHTS can bind both acetyl-CoA and succinyl-CoA and suggests that it may represent an intermediate between the succinate-transferring HTS family members and the acetate-transferring HTS family members. The B. cereus enzyme was unable to rescue growth of an Escherichia coli strain lacking a functional transsuccinylase, however.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2007.07.044