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

Characterization of the S289A,D mutants of yeast cystathionine beta-synthase.

Biochimica et biophysica acta - 1 Jun 2009

Quazi Faraz, Aitken Susan M

Abstract excerpt

Cystathionine beta-synthase (CBS) catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of l-serine and l-homocysteine to form l-cystathionine in the first step of the reverse transsulfuration pathway. Residue S289 of yeast CBS, predicted to form a hydrogen bond with the pyridine nitrogen of the PLP cofactor, was mutated to alanine and aspartate. The k(cat)/K(m)(l-Ser) of the S289A mutant is reduced...

Read the complete abstract on PubMed

Topics

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

Share to Biocatalysis
Share to Cystathionine beta-Synthase
Share to CBS gene

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

Share to Kinetics

Share to Mutation

Share to Pyridoxal Phosphate

Share to Spectrometry, Fluorescence

Share to Yeasts

Source

Identifiers

PMID: 19264153
DOI: 10.1016/j.bbapap.2009.02.007

Genes

CBS

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

Characterization of the S289A,D mutants of yeast cystathionine beta-synthase.PMID 19264153Read ↗

Residue N84 of yeast cystathionine beta-synthase is a determinant of reaction specificity.Semantic proximity Read ↗

Mutations in the regulatory domain of cystathionine beta-synthase can functionally suppress patient-derived mutations in cisSemantic proximity Read ↗

Domain architecture of the heme-independent yeast cystathionine beta-synthase provides insights into mechanisms of catalysis and regulation.Semantic proximity Read ↗

Structural insights into pathogenic mutations in heme-dependent cystathionine-beta-synthase.Semantic proximity Read ↗

Structural insights into mutations of cystathionine beta-synthase.Semantic proximity Read ↗

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

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

Characterization of two pathogenic mutations in cystathionine beta-synthase: different intracellular locations for wild-type and mutant proteins.Semantic proximity Read ↗

Functional modeling of vitamin responsiveness in yeast: a common pyridoxine-responsive cystathionine beta-synthase mutation in homocystinuria.Semantic proximity Read ↗

Visualization of PLP-bound intermediates in hemeless variants of human cystathionine beta-synthase: evidence that lysine 119 is a general base.Semantic proximity Read ↗

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

Insights into the regulatory domain of cystathionine Beta-synthase: characterization of six variant proteins.Semantic proximity Read ↗

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