Crystal structure of the pyridoxal‐5′‐phosphate‐dependent serine dehydratase from human liver
Crystal structure of the pyridoxal‐5′‐phosphate‐dependent serine dehydratase from human liver
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人肝脏吡哆醛-5′-磷酸依赖性丝氨酸脱水酶的晶体结构
DOI：
10.1110/ps.041179105
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发表时间：
2005
期刊：
影响因子：
8
通讯作者：
Z. Rao
中科院分区：
文献类型：
--
作者：
Lei Sun;M. Bartlam;Yiwei Liu;H. Pang;Z. Rao
L -丝氨酸脱水酶（SDH）是磷酸吡哆醛依赖酶(PLP) β家族的一员，可催化L -丝氨酸和L -苏氨酸脱氨生成丙酮酸或2 -氧丁酸盐。人肝脏L -丝氨酸脱水酶（hSDH）的晶体结构已通过分子置换在2.5 Å‐分辨率下解决。该结构为同型二聚体，并显示出β -家族PLP依赖性酶的典型折叠。每个单体作为活性单元，被细分为两个不同的结构域：一个小结构域和一个共价锚定辅因子的PLP结合结构域。这两个结构域都表现出PLP酶典型的开放α/β结构。与rSDH‐（PLP‐OMS）全酶相比，人工O‐甲基丝氨酸引起的活性位点结构差异较大。进一步测定了hSDH - PLP的活性，证明其具有催化活性。这表明hSDH - PLP的结构是天然活性holo - SDH的第一种结构。
L‐serine dehydratase (SDH), a member of the β‐family of pyridoxal phosphate‐dependent (PLP) enzymes, catalyzes the deamination of L‐serine and L‐threonine to yield pyruvate or 2‐oxobutyrate. The crystal structure of L‐serine dehydratase from human liver (hSDH) has been solved at 2.5 Å‐resolution by molecular replacement. The structure is a homodimer and reveals a fold typical for β‐family PLP‐dependent enzymes. Each monomer serves as an active unit and is subdivided into two distinct domains: a small domain and a PLP‐binding domain that covalently anchors the cofactor. Both domains show the typical open α/β architecture of PLP enzymes. Comparison with the rSDH‐(PLP‐OMS) holo‐enzyme reveals a large structural difference in active sites caused by the artifical O‐methylserine. Furthermore, the activity of hSDH‐PLP was assayed and it proved to show catalytic activity. That suggests that the structure of hSDH‐PLP is the first structure of the active natural holo‐SDH.
人结肠癌和大鼠肉瘤中丝氨酸代谢中的酶不平衡。
影响因子：
8.8
作者：
Snell, K;Natsumeda, Y;Eble, J N;Glover, J L;Weber, G
通讯作者：
Weber, G
钾离子对大肠杆菌 D-丝氨酸脱水酶吡哆醛 5-磷酸辅因子磷 31 核磁共振谱的影响。
影响因子：
3.9
作者：
Kojiro,CL;Marceau,M;Shafer,JA
通讯作者：
Shafer,JA