Structure of human cystathionine β-synthase:: a unique pyridoxal 5′-phosphate-dependent heme protein
Structure of human cystathionine β-synthase:: a unique pyridoxal 5′-phosphate-dependent heme protein
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DOI：
10.1093/emboj/20.15.3910
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发表时间：
2001-08-01
期刊：
影响因子：
11.4
通讯作者：
Burkhard, P
中科院分区：
文献类型：
--
作者：
Meier, M;Janosik, M;Burkhard, P
胱硫醚β-合酶（CBS）是一种独特的含血红素的酶，其催化丝氨酸和高半胱氨酸的吡哆醛5 ' -磷酸（PLP）依赖性缩合以产生胱硫醚。CBS缺乏导致同型胱氨酸尿症，这是一种硫代谢的遗传性疾病，其特征在于毒性代谢产物同型半胱氨酸水平升高。在这里，我们提出的X-射线晶体结构的截断形式的酶。CBS与O-乙酰丝氨酸硫化氢解酶具有相同的折叠，但它含有额外的N-末端血红素结合位点。这个血红素结合基序与空间相邻的氧化还原酶活性位点基序一起可以解释其酶活性的调节通过氧化还原变化。
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.