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Article

pH-dependent properties of a mutant horseradish peroxidase isoenzyme C in which Arg38 has been replaced with lysine.

European journal of biochemistry - 15 Sept 1994

Sanders S A, Bray R C, Smith A T

Abstract excerpt

Arg38 in the active site of horseradish peroxidase isoenzyme C (HRP-C) has been replaced with lysine by site-directed mutagenesis. As a preclude to a detailed kinetic analysis of this variant, the present study characterizes a pH-dependent cycle of reactions for recombinant horseradish peroxidase isoenzyme C with Arg38 replaced by lysine ([R38K]HRP-C*), which involves time-dependent changes in both specific...

Topics

Arginine
Binding Sites
Horseradish Peroxidase
Hydrogen-Ion Concentration
Isoenzymes
Kinetics
Lysine
Mutation
Plants
Spectrum Analysis

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Identifiers

PMID: 7925400
DOI: 10.1111/j.1432-1033.1994.01029.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7925400-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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