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Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein.


ABSTRACT: Cystathionine beta-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.

SUBMITTER: Meier M 

PROVIDER: S-EPMC149156 | biostudies-literature | 2001 Aug

REPOSITORIES: biostudies-literature

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Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein.

Meier M M   Janosik M M   Kery V V   Kraus J P JP   Burkhard P P  

The EMBO journal 20010801 15


Cystathionine beta-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  ...[more]

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