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Article

Catalytic and potentiometric characterization of E201D and E201Q mutants of Trypanosoma congolense trypanothione reductase.

Biochemistry - 3 Oct 1995

Zheng R, Cenas N, Blanchard J S

Abstract excerpt

Trypanothione reductase is a member of the structurally and functionally well-characterized family of flavoprotein reductases, which catalyze the reduced pyridine nucleotide dependent reduction of their disulfide, peroxide, or metal ion substrates. Trypanothione reductase is found in a wide variety of Trypanosoma species, where the enzyme serves physiologically to protect the organism from oxidative stress and...

Topics

Animals
Base Sequence
Catalysis
Electrochemistry
Kinetics
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
NADH, NADPH Oxidoreductases
Nucleotides
Oxidation-Reduction

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Substrate Specificity

Trypanosoma congolense

Source

Identifiers

PMID: 7548022
DOI: 10.1021/bi00039a028

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7548022-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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