期刊
EMBO JOURNAL
卷 20, 期 15, 页码 3910-3916出版社
OXFORD UNIV PRESS
DOI: 10.1093/emboj/20.15.3910
关键词
cystathionine beta-synthase; cysteine biosynthesis; heme protein; pyridoxal 5 '-phosphate; X-ray crystal structure
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据