Leucine dehydrogenase from Bacillus stearothermophilus: identification of active-site lysine by modification with pyridoxal phosphate.

doi:10.1093/oxfordjournals.jbchem.a123887

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Article

Leucine dehydrogenase from Bacillus stearothermophilus: identification of active-site lysine by modification with pyridoxal phosphate.

Journal of biochemistry - 1 Aug 1992

Matsuyama T, Soda K, Fukui T, Tanizawa K

Abstract excerpt

We have constructed an efficient expression plasmid for the leucine dehydrogenase gene previously cloned from Bacillus stearothermophilus. The recombinant enzyme was overproduced in Escherichia coli cells to a level of more than 30% of the total soluble protein upon induction with isopropyl beta-...

Topics

Amino Acid Oxidoreductases
Amino Acid Sequence
Base Sequence
Binding Sites
Borohydrides
Geobacillus stearothermophilus
Leucine Dehydrogenase
Lysine
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Plasmids
Pyridoxal Phosphate

Source

Open in PubMed

Identifiers

PMID: 1400267
DOI: 10.1093/oxfordjournals.jbchem.a123887

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1400267-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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