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Substrate specificity and identification of functional groups of homoserine kinase from Escherichia coli.

Abstract：

:Homoserine kinase, an enzyme in the aspartate pathway of amino acid biosynthesis in Escherichia coli, catalyzes the conversion of L-homoserine to L-homoserine phosphate. This enzyme has been found to have broad substrate specificity, including the phosphorylation of L-homoserine analogs where the carboxyl functional group at the alpha-position has been replaced by an ester or by a hydroxymethyl group. Previous pH profile studies [Huo. X., & Viola, R. E. (1996) Arch. Biochem. Biophys. 330, 373-379] and chemical modification studies have suggested the involvement of histidinyl, lysyl, and argininyl residues in the catalytic activity of the enzyme. With the assistance of sequence alignments, several potential amino acids have been targeted for examination. Site-directed mutagenesis studies have confirmed a role for arginine-234 in the binding of the carboxyl group of L-homoserine, and the involvement of two histidine at the homoserine binding site. Mutations at these sites have led to the decoupling of the kinase activity from an inherent ATPase activity in the enzyme, and suggest the presence of independent domains for the binding of each substrate in homoserine kinase.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Huo X,Viola RE

doi

10.1021/bi962203z

subject

Has Abstract

pub_date

1996-12-17 00:00:00

pages

16180-5

issue

50

eissn

0006-2960

issn

1520-4995

pii

bi962203z

journal_volume

35

pub_type

杂志文章

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