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

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

Biochemistry - 18 Dec 2007

Rao K Sudhindra, Fu Zhuji, Albro Mark, Narayanan Beena, Baddam Saritha, Lee Hyun-Joo K, Kim Jung-Ja P, Frerman Frank E

Abstract excerpt

We have determined steady-state rate constants and net rate constants for the chemical steps in the catalytic pathway catalyzed by the E370D mutant of glutaryl-CoA dehydrogenase and compared them with those of the wild-type dehydrogenase. We sought rationales for changes in these rate constants in the structure of the mutant cocrystallized with the alternate substrate, 4-nitrobutyric acid. Substitution of...

Read the complete abstract on PubMed

Topics

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

Share to Acyl Coenzyme A
Share to Aspartic Acid

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

Share to Chromatography, High Pressure Liquid

Share to Crystallography

Share to Glutamic Acid

Share to Glutaryl-CoA Dehydrogenase

Share to Mass Spectrometry

Share to Protons

Source

Identifiers

PMID: 18020372
DOI: 10.1021/bi7009597

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

The effect of a Glu370Asp mutation in glutaryl-CoA dehydrogenase on proton transfer to the dienolate intermediate.PMID 18020372Read ↗

The function of Arg-94 in the oxidation and decarboxylation of glutaryl-CoA by human glutaryl-CoA dehydrogenase.Semantic proximity Read ↗

Pathogenic mutations in the carboxyl-terminal domain of glutaryl-CoA dehydrogenase: effects on catalytic activity and the stability of the tetramer.Semantic proximity Read ↗

Ability of single-site mutants of citrate synthase to catalyze proton transfer from the methyl group of dethiaacetyl-coenzyme A, a non-thioester substrate analog.Semantic proximity Read ↗

Hydride Transfer Catalyzed by Glycerol Phosphate Dehydrogenase: Recruitment of an Acidic Amino Acid Side Chain to Rescue a Damaged Enzyme.Semantic proximity Read ↗

Significant catalytic roles for Glu47 and Gln 110 in all four of the C-C bond-making and -breaking steps of the reactions of acetohydroxyacid synthase II.Semantic proximity Read ↗

Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multienzyme complex.Semantic proximity Read ↗

A carboxylate switch point controls long-range energy transduction in respiratory Complex I.Semantic proximity Read ↗

Dual roles of Lys(57) at the dimer interface of human mitochondrial NAD(P)+-dependent malic enzyme.Semantic proximity Read ↗

Structural mutations that probe the interactions between the catalytic and dianion activation sites of triosephosphate isomerase.Semantic proximity Read ↗

A Carboxylate Switch Point Controls Long-Range Energy Transduction in Respiratory Complex ISemantic proximity Read ↗

A Suicide Mutation Affecting Proton Transfers to High-Valent Hemes Causes Inactivation of MauG during Catalysis.Semantic proximity Read ↗

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

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