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

Hydrogen deuterium exchange defines catalytically linked regions of protein flexibility in the catechol O-methyltransferase reaction.

Proceedings of the National Academy of Sciences of the United States of America - 19 May 2020

Zhang Jianyu, Balsbaugh Jeremy L, Gao Shuaihua, Ahn Natalie G, Klinman Judith P

Abstract excerpt

Human catechol O-methyltransferase (COMT) has emerged as a model for understanding enzyme-catalyzed methyl transfer from S-adenosylmethionine (AdoMet) to small-molecule catecholate acceptors. Mutation of a single residue (tyrosine 68) behind the methyl-bearing sulfonium of AdoMet was previously shown to impair COMT activity by interfering with methyl donor-acceptor compaction within the activated ground state of...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catechol O-Methyltransferase

Share to Molecular Dynamics Simulation

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 32371482
DOI: 10.1073/pnas.1917219117
PMCID: PMC7245127

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Hydrogen deuterium exchange defines catalytically linked regions of protein flexibility in the catechol O-methyltransferase reaction.PMID 32371482Read ↗

Convergent Mechanistic Features between the Structurally Diverse N- and O-Methyltransferases: Glycine N-Methyltransferase and Catechol O-Methyltransferase.Semantic proximity Read ↗

The 108M polymorph of human catechol O-methyltransferase is prone to deformation at physiological temperatures.Semantic proximity Read ↗

Nano-second protein dynamics of key residue at Position 38 in catechol-O-methyltransferase system: a time-resolved fluorescence study.Semantic proximity Read ↗

Identification of Thermal Conduits That Link the Protein-Water Interface to the Active Site Loop and Catalytic Base in Enolase.Semantic proximity Read ↗

Factor VIII-driven changes in activated factor IX explored by hydrogen-deuterium exchange mass spectrometry.Semantic proximity Read ↗

The V108M mutation decreases the structural stability of catechol O-methyltransferase.Semantic proximity Read ↗

Insights into the pathogenesis of primary hyperoxaluria type I from the structural dynamics of alanine:glyoxylate aminotransferase variants.Semantic proximity Read ↗

Active site tyrosine residues in human NQO1 homodimer are critical for non-synchronous enzyme catalysis at the two active sitesSemantic proximity Read ↗

The unique functional role of the C-HS hydrogen bond in the substrate specificity and enzyme catalysis of type 1 methionine aminopeptidase.Semantic proximity Read ↗

Hydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter.Semantic proximity Read ↗

A remote mutation affects the hydride transfer by disrupting concerted protein motions in thymidylate synthase.Semantic proximity Read ↗

Catalytic Reaction Mechanism in Native and Mutant Catechol- O-methyltransferase from the Adaptive String Method and Mean Reaction Force Analysis.Semantic proximity Read ↗

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