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Article

Evidence for lysine 80 as general base catalyst of leucine dehydrogenase.

The Journal of biological chemistry - 25 Dec 1993

Sekimoto T, Matsuyama T, Fukui T, Tanizawa K

Abstract excerpt

To elucidate the functional role of the lysyl residue highly conserved in NAD(P)(+)-dependent amino acid dehydrogenases, Lys-80 of leucine dehydrogenase from Bacillus stearothermophilus has been mutated into Ala, Arg, or Gln. All of the mutant enzymes had markedly reduced activities in the oxidative deamination, whereas the Michaelis constants for substrate and coenzyme did not change significantly upon the...

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Source

Identifiers

PMID: 8262941

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Evidence for lysine 80 as general base catalyst of leucine dehydrogenase.PMID 8262941Read ↗

Tyrosine 70 fine-tunes the catalytic efficiency of aspartate aminotransferase.Semantic proximity Read ↗

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

The role of substrate-binding groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase.Semantic proximity Read ↗

Attempting to remove the substrate inhibition of L-lactate dehydrogenase from Bacillus stearothermophilus by site-directed mutagenesis.Semantic proximity Read ↗

Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida tenuis xylose reductase (AKR2B5) probed by site-directed mutagenesis and functional complementation studies.Semantic proximity Read ↗

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

Substitution of apolar residues in the active site of aspartate aminotransferase by histidine. Effects on reaction and substrate specificity.Semantic proximity Read ↗

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Histidine-40 of ribonuclease T1 acts as base catalyst when the true catalytic base, glutamic acid-58, is replaced by alanine.Semantic proximity Read ↗

Mutation of arginine 98, which serves as a substrate-recognition site of D-amino acid aminotransferase, can be partly compensated for by mutation of tyrosine 88 to an arginyl residue.Semantic proximity Read ↗

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