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Article

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

Biochemical and biophysical research communications - 16 Mar 1990

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

Abstract excerpt

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 f...

Topics

Aspartate Aminotransferases
Circular Dichroism
Escherichia coli
Glycine
Kinetics
Mutation
Phenylalanine
Protein Conformation
Spectrophotometry
Substrate Specificity
Tryptophan

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Identifiers

PMID: 2182010
DOI: 10.1016/0006-291x(90)92037-z

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-2182010-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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