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Effects of replacement of tryptophan-140 by phenylalanine or glycine on the function of Escherichia coli aspartate aminotransferase.

Abstract：

:Trp140 of E. coli aspartate aminotransferase has been converted to Phe or Gly by site-directed mutagenesis. As compared to the wild-type enzyme, either of the mutant enzymes showed 10- to 100-fold increase in Km's for natural dicarboxylic substrates, but did not show appreciable changes in Km's for aromatic substrates. Teh kcat values for dicarboxylic and aromatic substrates were greatly decreased by [Trp140----Gly] mutation, but were decreased to lesser extents by [Trp140----Phe] mutation. These findings suggested that N(1) of Trp140 may not be essential for catalysis, but may be partly involved in the binding of the distal carboxylate group of the dicarboxylic substrates.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Hayashi H,Inoue Y,Kuramitsu S,Morino Y,Kagamiyama H

doi

10.1016/0006-291x(90)92037-z

subject

Has Abstract

pub_date

1990-03-16 00:00:00

pages

407-12

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(90)92037-Z

journal_volume

167

pub_type

杂志文章

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