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Article

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

Proceedings of the National Academy of Sciences of the United States of America - 16 Sept 2014

Ereño-Orbea June, Majtan Tomas, Oyenarte Iker, Kraus Jan P, Martínez-Cruz Luis Alfonso

Abstract excerpt

Cystathionine β-synthase (CBS) is a heme-dependent and pyridoxal-5'-phosphate-dependent protein that controls the flux of sulfur from methionine to cysteine, a precursor of glutathione, taurine, and H2S. Deficiency of CBS activity causes homocystinuria, the most frequent disorder of sulfur amino acid metabolism. In contrast to CBSs from lower organisms, human CBS (hCBS) is allosterically activated by...

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Share to Allosteric Regulation
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Enzyme Stability

Share to Protein Interaction Domains and Motifs

Share to Protein Interaction Mapping

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Source

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Identifiers

PMID: 25197074
DOI: 10.1073/pnas.1414545111
PMCID: PMC4169959

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.

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