Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Arginine
Share to Binding Sites
Share to Hydrogen-Ion Concentration

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Isoenzymes

Share to Kinetics

Share to Lysine

Share to Mutation

Share to Plants

Source

Identifiers

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

Provenance

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

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

pH-dependent properties of a mutant horseradish peroxidase isoenzyme C in which Arg38 has been replaced with lysine.PMID 7925400Read ↗

Characterisation of a haem active-site mutant of horseradish peroxidase, Phe41----Val, with altered reactivity towards hydrogen peroxide and reducing substrates.Semantic proximity Read ↗

Role of the K-channel in the pH-dependence of the reaction of cytochrome c oxidase with hydrogen peroxide.Semantic proximity Read ↗

Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis.Semantic proximity Read ↗

Characterization of the hydrogen peroxide-enzyme reaction for two cytochrome c peroxidase mutants.Semantic proximity Read ↗

Identification of a critical phenylalanine residue in horseradish peroxidase, Phe179, by site-directed mutagenesis and 1H-NMR: implications for complex formation with aromatic donor molecules.Semantic proximity Read ↗

Versatility of non-native forms of human cytochrome c: pH and micellar concentration dependence.Semantic proximity Read ↗

Investigating the structural and functional effects of mutating Asn glycosylation sites of horseradish peroxidase to Asp.Semantic proximity Read ↗

Structural and functional characterization of phosphomimetic mutants of cytochrome c at threonine 28 and serine 47.Semantic proximity Read ↗

Effects of mutations in the helix G region of horseradish peroxidase.Semantic proximity Read ↗

On the role of the K-proton transfer pathway in cytochrome c oxidase.Semantic proximity Read ↗

The Catalase Activity of Catalase-Peroxidases Is Modulated by Changes in the pKa of the Distal Histidine.Semantic proximity Read ↗

Relocation of an internal proton donor in cytochrome c oxidase results in an altered pK(a) and a non-integer pumping stoichiometry.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.