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

Histidine-alpha143 assists 1,2-hydroxyl group migration and protects radical intermediates in coenzyme B12-dependent diol dehydratase.

Biochemistry - 11 Mar 2008

Kinoshita Koichiro, Kawata Masahiro, Ogura Ken-ichi, Yamasaki Ai, Watanabe Takeshi, Komoto Noriaki, Hieda Naoki, Yamanishi Mamoru, Tobimatsu Takamasa, Toraya Tetsuo

Abstract excerpt

Diol dehydratase of Klebsiella oxytoca contains an essential histidine residue. Its X-ray structure revealed that the migrating hydroxyl group on C2 of substrate is hydrogen-bonded to Hisalpha143. Mutant enzymes in which Hisalpha143 was mutated to another amino acid residue were expressed in Esch...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography, X-Ray
Share to Electron Spin Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Histidine

Share to Hydrogen Bonding

Share to Hydrogen-Ion Concentration

Share to Molecular Structure

Share to Structure-Activity Relationship

Share to Substrate Specificity

Source

Identifiers

PMID: 18260646
DOI: 10.1021/bi7018095

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-18260646-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Histidine-alpha143 assists 1,2-hydroxyl group migration and protects radical intermediates in coenzyme B12-dependent diol dehydratase.PMID 18260646Read ↗

Computational mutation analysis of hydrogen abstraction and radical rearrangement steps in the catalysis of coenzyme B12-dependent diol dehydratase.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 ↗

Role of tyrosine 143 in lactate dehydrogenation by flavocytochrome b2. Primary kinetic isotope effect studies with a phenylalanine mutant.Semantic proximity Read ↗

Redesign of coenzyme B(12) dependent diol dehydratase to be resistant to the mechanism-based inactivation by glycerol and act on longer chain 1,2-diols.Semantic proximity Read ↗

Studies of the mechanism of the delta 5-3-ketosteroid isomerase reaction by substrate, solvent, and combined kinetic deuterium isotope effects on wild-type and mutant enzymes.Semantic proximity Read ↗

Product deuterium isotope effects for orotidine 5'-monophosphate decarboxylase: effect of changing substrate and enzyme structure on the partitioning of the vinyl carbanion reaction intermediate.Semantic proximity Read ↗

Effect of Lys84 carbamylation and chloride ion on OXA-143 dynamics and catalytic efficiencySemantic proximity Read ↗

Decarboxylation involving a ferryl, propionate, and a tyrosyl group in a radical relay yields heme b.Semantic proximity Read ↗

When a spectator turns killer: suicidal electron transfer from cobalamin in methylmalonyl-CoA mutase.Semantic proximity Read ↗

Role of Histidine-152 in cofactor orientation in the PLP-dependent O-acetylserine sulfhydrylase reaction.Semantic proximity Read ↗

A catalytic consensus motif for D-mannitol 2-dehydrogenase, a member of a polyol-specific long-chain dehydrogenase family, revealed by kinetic characterization of site-directed mutants of the enzyme from Pseudomonas fluorescens.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.