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B6db references: 21376038

type Journal Article
authors Meier, M.; Janosik, M.; Kery, V.; Kraus, J. P.; Burkhard, P.
title Structure of human cystathionine beta-synthase: a unique pyridoxal 5'- phosphate-dependent heme protein
journal Embo J
ui 21376038
year (2001)
volume 20
number 15
pages 3910-6.
keywords Amino Acid Sequence
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.
last changed 2002/11/12 16:17

B6db references