Alteration in relative activities of phenylalanine dehydrogenase towards different substrates by site-directed mutagenesis

Glycine-124 and leucine-307 of phenylalanine dehydrogenase from Bacillus sphaericus were altered by site-specific mutagenesis to the corresponding residues in leucine dehydrogenase: alanine and valine, respectively. These two residues have previously been implicated from molecular modelling as impor...

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Bibliographic Details
Published in:FEBS letters 1995-08, Vol.370 (1), p.93-96
Main Authors: Seah, Stephen Y.K., Linda Britton, K., Baker, Patrick J., Rice, David W., Asano, Yasuhisa, Engel, Paul C.
Format: Article
Language:English
Subjects:
Amino Acid Oxidoreductases - biosynthesis
Amino Acid Oxidoreductases - chemistry
Amino Acid Oxidoreductases - metabolism
Amino Acid Sequence
Amino acids
Amino Acids - metabolism
Bacillus - enzymology
Base Sequence
Glycine
Kinetics
Leucine
Leucine Dehydrogenase
Models, Molecular
Molecular Sequence Data
Mutagenesis
Mutagenesis, Site-Directed
Oligodeoxyribonucleotides
Phenylalanine dehydrogenase
Point Mutation
Protein Conformation
Recombinant Proteins - biosynthesis
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Substrate Specificity
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Summary:Glycine-124 and leucine-307 of phenylalanine dehydrogenase from Bacillus sphaericus were altered by site-specific mutagenesis to the corresponding residues in leucine dehydrogenase: alanine and valine, respectively. These two residues have previously been implicated from molecular modelling as important in determining the substrate discrimination of the two enzymes. Single and double mutants displayed lower activities towards l-phenylalanine and enhanced activity towards almost all aliphatic amino acid substrates tested compared to the wild-type, thus confirming the predictions made from molecular modelling.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(95)00804-I