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

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

Chemistry (Weinheim an der Bergstrasse, Germany) - 1 Jan 2007

Kamachi Takashi, Toraya Tetsuo, Yoshizawa Kazunari

Abstract excerpt

A mutation analysis of the catalytic functions of active-site residues of coenzyme B(12)-dependent diol dehydratase in the conversion of 1,2-propanediol to 1,1-propanediol has been carried out by using QM/MM computations. Mutants His143Ala, Glu170Gln, Glu170Ala, and Glu170Ala/Glu221Ala were considered to estimate the impact of the mutations of His143 and Glu170. In the His143Ala mutant the activation energy for...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Catalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Computational Biology

Share to DNA Mutational Analysis

Share to Enzyme Activation

Share to Hydrogen

Share to Protein Conformation

Share to Vitamin B 12

Source

Identifiers

PMID: 17614304
DOI: 10.1002/chem.200601466

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Computational mutation analysis of hydrogen abstraction and radical rearrangement steps in the catalysis of coenzyme B12-dependent diol dehydratase.PMID 17614304Read ↗

[Computational mutation analysis of enzymatic reaction].Semantic proximity Read ↗

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

Crystal structure of aldoxime dehydratase and its catalytic mechanism involved in carbon-nitrogen triple-bond synthesis.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 ↗

Reconstructing dynamics correlation network to simultaneously improve activity and stability of 2,3-butanediol dehydrogenase by design of distal interchain disulfide bonds.Semantic proximity Read ↗

Role of a mutated residue at the entrance of the substrate access channel in cytochrome p450 engineered for vitamin D(3) hydroxylation activity.Semantic proximity Read ↗

Just an additional hydrogen bond can dramatically reduce the catalytic activity of Bacillus subtilis lipase A I12T mutant: an integration of computational modeling and experimental analysis.Semantic proximity Read ↗

Catalytic mechanism and product specificity of oxidosqualene-lanosterol cyclase: a QM/MM study.Semantic proximity Read ↗

Mutation of Lys242 allows Delta3-Delta2-enoyl-CoA isomerase to acquire enoyl-CoA hydratase activity.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 ↗

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 ↗

Contributions of long-range electrostatic interactions to 4-chlorobenzoyl-CoA dehalogenase catalysis: a combined theoretical and experimental study.Semantic proximity Read ↗

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