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

Asp338 controls hydride transfer in Escherichia coli IMP dehydrogenase.

Biochemistry - 15 Aug 2000

Kerr K M, Digits J A, Kuperwasser N, Hedstrom L

Abstract excerpt

IMP dehydrogenase (IMPDH) catalyzes the oxidation of IMP to XMP with the concomitant reduction of NAD(+). This reaction involves the formation of a covalent adduct with an active site Cys. This intermediate, E-XMP, hydrolyzes to produce XMP. The mutation of Asp338 to Ala severely impairs the activity of Escherichia coli IMPDH, decreasing the value of k(cat) by 650-fold. No (D)V(m) or (D)V/K(m) isotope effects are...

Read the complete abstract on PubMed

Topics

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

Share to Alkylation
Share to Aspartic Acid
Share to Catalysis

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

Share to Catalytic Domain

Share to Deuterium

Share to Hydrogen

Share to IMP Dehydrogenase

Share to Models, Chemical

Source

Identifiers

PMID: 10933797
DOI: 10.1021/bi0005409

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

Asp338 controls hydride transfer in Escherichia coli IMP dehydrogenase.PMID 10933797Read ↗

Identification of a region involved in the communication between the NADP(H) binding domain and the membrane domain in proton pumping E. coli transhydrogenase.Semantic proximity Read ↗

Site-directed mutagenesis of the regulatory domain of Escherichia coli carbamoyl phosphate synthetase identifies crucial residues for allosteric regulation and for transduction of the regulatory signals.Semantic proximity Read ↗

A functional analysis of the allosteric nucleotide monophosphate binding site of carbamoyl phosphate synthetase.Semantic proximity Read ↗

Residues distal from the active site that alter enzyme function in M.HhaI DNA cytosine methyltransferase.Semantic proximity Read ↗

Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human mitochondrial NAD(P)+-dependent malate dehydrogenase (malic enzyme).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 ↗

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

Glutamate 270 plays an essential role in K(+)-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase.Semantic proximity Read ↗

Redox-sensitive loops D and E regulate NADP(H) binding in domain III and domain I-domain III interactions in proton-translocating Escherichia coli transhydrogenase.Semantic proximity Read ↗

Dual Role of the Active Site Residues of Thermus thermophilus 3-Isopropylmalate Dehydrogenase: Chemical Catalysis and Domain Closure.Semantic proximity Read ↗

The effective molarity of the substrate phosphoryl group in the transition state for yeast OMP decarboxylase.Semantic proximity Read ↗

The CBS subdomain of inosine 5'-monophosphate dehydrogenase regulates purine nucleotide turnover.Semantic proximity Read ↗

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