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

Role of asparagine 510 in the relative timing of substrate bond cleavages in the reaction catalyzed by choline oxidase.

Biochemistry - 23 Mar 2010

Rungsrisuriyachai Kunchala, Gadda Giovanni

Abstract excerpt

The flavoprotein choline oxidase catalyzes the oxidation of choline to glycine betaine with transient formation of an aldehyde intermediate and molecular oxygen as final electron acceptor. The enzyme has been grouped in the glucose-methanol-choline oxidoreductase enzyme superfamily, which shares a highly conserved His-Asn catalytic pair in the active site. In this study, the conserved asparagine residue at...

Read the complete abstract on PubMed

Topics

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

Share to Alcohol Oxidoreductases
Share to Asparagine
Share to Biocatalysis

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

Share to Catalytic Domain

Share to Flavins

Share to Mutagenesis, Site-Directed

Share to Oxidation-Reduction

Share to Spectrum Analysis

Source

Identifiers

PMID: 20163155
DOI: 10.1021/bi901796a

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

Role of asparagine 510 in the relative timing of substrate bond cleavages in the reaction catalyzed by choline oxidase.PMID 20163155Read ↗

Structural and kinetic studies on the Ser101Ala variant of choline oxidase: catalysis by compromise.Semantic proximity Read ↗

Role of Glu312 in binding and positioning of the substrate for the hydride transfer reaction in choline oxidase.Semantic proximity Read ↗

Evidence for proton tunneling and a transient covalent flavin-substrate adduct in choline oxidase S101A.Semantic proximity Read ↗

Effect of a conservative mutation of an active site residue involved in substrate binding on the hydride tunneling reaction catalyzed by choline oxidase.Semantic proximity Read ↗

Rescuing of the hydride transfer reaction in the Glu312Asp variant of choline oxidase by a substrate analogue.Semantic proximity Read ↗

Effects of reversing the protein positive charge in the proximity of the flavin N(1) locus of choline oxidase.Semantic proximity Read ↗

The effect of a Glu370Asp mutation in glutaryl-CoA dehydrogenase on proton transfer to the dienolate intermediate.Semantic proximity Read ↗

Role of F357 as an Oxygen Gate in the Oxidative Half-Reaction of Choline Oxidase.Semantic proximity Read ↗

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

Cysteine-191 in aspartate aminotransferases appears to be conserved due to the lack of a neutral mutation pathway to the functional equivalent, alanine-191.Semantic proximity Read ↗

Role of a strictly conserved active site tyrosine in cofactor genesis in the copper amine oxidase from Hansenula polymorpha.Semantic proximity Read ↗

The roles of Tyr70 and Tyr225 in aspartate aminotransferase assessed by analysing the effects of mutations on the multiple reactions of the substrate analogue serine o-sulphate.Semantic proximity Read ↗

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