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

Interaction with the Redox Cofactor MYW and Functional Role of a Mobile Arginine in Eukaryotic Catalase-Peroxidase.

Biochemistry - 28 Jun 2016

Gasselhuber Bernhard, Graf Michael M H, Jakopitsch Christa, Zamocky Marcel, Nicolussi Andrea, Furtmüller Paul G, Oostenbrink Chris, Carpena Xavi, Obinger Christian

Abstract excerpt

Catalase-peroxidases (KatGs) are unique bifunctional heme peroxidases with an additional posttranslationally formed redox-active Met-Tyr-Trp cofactor that is essential for catalase activity. On the basis of studies of bacterial KatGs, controversial mechanisms of hydrogen peroxide oxidation were proposed. The recent discovery of eukaryotic KatGs with differing pH optima of catalase activity now allows us to...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Calorimetry, Differential Scanning

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

Share to Circular Dichroism

Share to Hydrogen Peroxide

Share to Magnaporthe

Share to Molecular Dynamics Simulation

Share to Oxidants

Share to Peroxidases

Source

Open in PubMed Open full text

Identifiers

PMID: 27293030
DOI: 10.1021/acs.biochem.6b00436
PMCID: PMC4928148

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

Interaction with the Redox Cofactor MYW and Functional Role of a Mobile Arginine in Eukaryotic Catalase-Peroxidase.PMID 27293030Read ↗

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

Impact of distal side water and residue 315 on ligand binding to ferric Mycobacterium tuberculosis catalase-peroxidase (KatG).Semantic proximity Read ↗

Distinct roles of a tyrosine-associated hydrogen-bond network in fine-tuning the structure and function of heme proteins: two cases designed for myoglobin.Semantic proximity Read ↗

Two alternative substrate paths for compound I formation and reduction in catalase-peroxidase KatG from Burkholderia pseudomallei.Semantic proximity Read ↗

Evolution of Catalases from Bacteria to HumansSemantic proximity Read ↗

Distal site aspartate is essential in the catalase activity of catalase-peroxidases.Semantic proximity Read ↗

Role of conserved arginine in the heme distal site of HutZ from Vibrio cholerae in the heme degradation reaction.Semantic proximity Read ↗

Mutational effects on thermostable superoxide dismutase from Aquifex pyrophilus: understanding the molecular basis of protein thermostability.Semantic proximity Read ↗

Mutational dissection of a hole hopping route in a lytic polysaccharide monooxygenase (LPMO).Semantic proximity Read ↗

Mutual synergy between catalase and peroxidase activities of the bifunctional enzyme KatG is facilitated by electron hole-hopping within the enzyme.Semantic proximity Read ↗

Remarkable improvement of methylglyoxal synthase thermostability by His-His interaction.Semantic proximity Read ↗

Plasmodium falciparum glyoxalase II: Theorell-Chance product inhibition patterns, rate-limiting substrate binding via Arg(257)/Lys(260), and unmasking of acid-base catalysis.Semantic proximity Read ↗

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