Meier Markus, Oliveriusova Jana, Kraus Jan P, Burkhard Peter
M.E. Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056, Basel, Switzerland.
Biochim Biophys Acta. 2003 Apr 11;1647(1-2):206-13. doi: 10.1016/s1570-9639(03)00048-7.
Cystathionine beta-synthase (CBS) is a unique heme-containing enzyme that catalyses 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 amino acid metabolism characterised by increased levels of homocysteine and methionine and decreased levels of cysteine. Presently, more than 100 CBS mutations have been described which lead to homocystinuria with different degrees of severity in the patients. We have recently solved the crystal structure of a truncated form of this enzyme, which enables us to correlate some of these mutations with the structure.
胱硫醚β-合酶（CBS）是一种独特的含血红素酶，它催化丝氨酸和同型半胱氨酸的磷酸吡哆醛（PLP）依赖性缩合反应生成胱硫醚。CBS缺乏会导致同型胱氨酸尿症，这是一种硫氨基酸代谢的遗传性疾病，其特征是同型半胱氨酸和蛋氨酸水平升高，而半胱氨酸水平降低。目前，已经描述了100多种导致同型胱氨酸尿症的CBS突变，这些突变会使患者出现不同程度的病情严重程度。我们最近解析了这种酶截短形式的晶体结构，这使我们能够将其中一些突变与结构联系起来。
