Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein
Open Access
- 1 August 2001
- journal article
- research article
- Published by Springer Nature in The EMBO Journal
- Vol. 20 (15) , 3910-3916
- https://doi.org/10.1093/emboj/20.15.3910
Abstract
Cystathionine β‐synthase (CBS) is a unique heme‐ containing enzyme that catalyzes a pyridoxal 5′‐phosphate (PLP)‐dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Here we present the X‐ray crystal structure of a truncated form of the enzyme. CBS shares the same fold with O ‐acetylserine sulfhydrylase but it contains an additional N‐terminal heme binding site. This heme binding motif together with a spatially adjacent oxidoreductase active site motif could explain the regulation of its enzyme activity by redox changes.Keywords
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