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

Allosteric communication between the pyridoxal 5'-phosphate (PLP) and heme sites in the H2S generator human cystathionine β-synthase.

The Journal of biological chemistry - 2 Nov 2012

Yadav Pramod Kumar, Xie Peter, Banerjee Ruma

Abstract excerpt

Human cystathionine β-synthase (CBS) is a unique pyridoxal 5'-phosphate (PLP)-dependent enzyme that has a regulatory heme cofactor. Previous studies have demonstrated the importance of Arg-266, a residue at the heme pocket end of α-helix 8, for communication between the heme and PLP sites. In this study, we have examined the role of the conserved Thr-257 and Thr-260 residues, located at the other end of α-helix 8...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Cystathionine beta-Synthase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Homocystinuria

Share to Isomerism

Share to Pyridoxal Phosphate

Share to S-Adenosylmethionine

Share to Threonine

Source

Open in PubMed Open full text

Identifiers

PMID: 22977242
DOI: 10.1074/jbc.M112.414706
PMCID: PMC3488039

Genes

CBS

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

Allosteric communication between the pyridoxal 5'-phosphate (PLP) and heme sites in the H2S generator human cystathionine β-synthase.PMID 22977242Read ↗

Effect of the disease-causing R266K mutation on the heme and PLP environments of human cystathionine β-synthase.Semantic proximity Read ↗

Modulation of the heme electronic structure and cystathionine beta-synthase activity by second coordination sphere ligands: The role of heme ligand switching in redox regulation.Semantic proximity Read ↗

Disease-causing cystathionine β-synthase linker mutations impair allosteric regulation.Semantic proximity Read ↗

Understanding the Role of R266K Mutation in Cystathionine β-Synthase (CBS) Enzyme: An in Silico StudySemantic proximity Read ↗

Understanding the role of R266K mutation in cystathionine β-synthase (CBS) enzyme: an in silico study.Semantic proximity Read ↗

Structural insight into the molecular mechanism of allosteric activation of human cystathionine β-synthase by S-adenosylmethionine.Semantic proximity Read ↗

Structural basis of the dominant inheritance of hypermethioninemia associated with the Arg264His mutation in the MAT1A gene.Semantic proximity Read ↗

Mono and dual cofactor dependence of human cystathionine β-synthase enzyme variants in vivo and in vitro.Semantic proximity Read ↗

Effects of heme ligand mutations including a pathogenic variant, H65R, on the properties of human cystathionine beta-synthase.Semantic proximity Read ↗

Spectroscopic and kinetic studies of PKU-inducing mutants of phenylalanine hydroxylase: Arg158Gln and Glu280Lys.Semantic proximity Read ↗

Mechanism-based inhibition of human persulfide dioxygenase by γ-glutamyl-homocysteinyl-glycine.Semantic proximity Read ↗

Mapping peptides correlated with transmission of intrasteric inhibition and allosteric activation in human cystathionine beta-synthase.Semantic proximity Read ↗

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