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

Kinetics aspects of Gamma-hydroxybutyrate dehydrogenase.

Biochimica et biophysica acta. Proteins and proteomics - 1 May 2020

Taxon Esther S, Halbers Lila P, Parsons Stanley M

Abstract excerpt

Two groups of metabolically related enzymes, the Group III family of Fe2+-dependent alcohol dehydrogenases (ADHs) and the separate subfamily of nucleoside diphosphates linked to x (nudix) hydrolases that activate Group III ADHs are under-characterized. Here we report the steady-state initial-velocity forward direction (alcohol → aldehyde) reaction of a Group III ADH, namely gamma-hydroxybutyrate dehydrogenase...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Catalytic Domain
Share to Kinetics

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

Share to Mutation

Share to Pyrophosphatases

Source

Identifiers

PMID: 31981617
DOI: 10.1016/j.bbapap.2020.140376

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

Kinetics aspects of Gamma-hydroxybutyrate dehydrogenase.PMID 31981617Read ↗

In vitro activation of NAD-dependent alcohol dehydrogenases by Nudix hydrolases is more widespread than assumed.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 ↗

Drosophila alcohol dehydrogenase: acetate-enzyme interactions and novel insights into the effects of electrostatics on catalysis.Semantic proximity Read ↗

Evolution of Glucose Dehydrogenase for Cofactor Regeneration in Bioredox Processes with Denaturing Agents.Semantic proximity Read ↗

Novel dehydrogenase catalyzes oxidative hydrolysis of carbon-nitrogen double bonds for hydrazone degradation.Semantic proximity Read ↗

Purification of two putative type II NADH dehydrogenases with different substrate specificities from alkaliphilic Bacillus pseudofirmus OF4.Semantic proximity Read ↗

Identification of a novel NADH-specific aldo-keto reductase using sequence and structural homologies.Semantic proximity Read ↗

Characterization of active site variants of xanthine hydroxylase from Aspergillus nidulans.Semantic proximity Read ↗

Expanding the cofactor range of aldehyde reductase YqhD by mutating key amino acids.Semantic proximity Read ↗

Identification of a magnesium-dependent NAD(P)(H)-binding domain in the nicotinoprotein methanol dehydrogenase from Bacillus methanolicus.Semantic proximity Read ↗

Allosteric regulation of glutamate dehydrogenase deamination activity.Semantic proximity Read ↗

The β2αB loop determines NAD(P) cofactor specificity and kinetics in trypanosomal D-3-hydroxybutyrate dehydrogenases.Semantic proximity Read ↗

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