Role of leucine 201 of thermostable D-amino acid aminotransferase from a thermophile, Bacillus sp. YM-1.

doi:10.1093/oxfordjournals.jbchem.a124765

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Article

Role of leucine 201 of thermostable D-amino acid aminotransferase from a thermophile, Bacillus sp. YM-1.

Journal of biochemistry - 1 Apr 1995

Kishimoto K, Yoshimura T, Esaki N, Sugio S, Manning J M, Soda K

Abstract excerpt

We studied the catalytic role of leucine 201 residue of the thermostable D-amino acid aminotransferase: the residue was shown crystallographically to be in the vicinity of the active site to interact with the bound pyridoxal phosphate. We replaced the leucine 201 by alanyl or tryptophanyl residue...

Topics

Alanine
Alanine Transaminase
Bacillus
Bacterial Proteins
Base Sequence
Binding Sites
Catalysis
Circular Dichroism
D-Alanine Transaminase
Enzyme Activation
Enzyme Stability
Hot Temperature

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Kinetics

Leucine

Molecular Sequence Data

Mutation

Pyridoxal Phosphate

Pyridoxamine

Source

Open in PubMed

Identifiers

PMID: 7592528
DOI: 10.1093/oxfordjournals.jbchem.a124765

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7592528-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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