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Article

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

Human mutation - 1 Oct 2014

Mendes Marisa I S, Santos Ana Sofia, Smith Desirée E C, Lino Paulo Roque, Colaço Henrique G, de Almeida Isabel Tavares, Vicente João B, Salomons Gajja S, Rivera Isabel, Blom Henk J, Leandro Paula

Abstract excerpt

Cystathionine beta-synthase (CBS) catalyzes the formation of cystathionine from homocysteine and serine. CBS is allosterically activated by S-adenosylmethionine (SAM), which binds to its C-terminal regulatory domain. Mutations in this domain lead to variants with high residual activity but lacking SAM activation. We characterized six C-terminal CBS variants (p.P427L, p.D444N, p.V449G, p.S500L, p.K523Sfs*18, and...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 25044645
DOI: 10.1002/humu.22616

Genes

CBS

Variants

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.

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