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
Activity	4.2.1.22
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