与抑制剂5-羟基戊酸复合的酵母5-氨基乙酰丙酸脱水酶的结构
Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid.
作者信息
Erskine P T, Coates L, Newbold R, Brindley A A, Stauffer F, Beaven G D E, Gill R, Coker A, Wood S P, Warren M J, Shoolingin-Jordan P M, Neier R, Cooper J B
机构信息
School of Biological Sciences, University of Southampton, Bassett Crescent East, Southampton SO16 7PX, England.
出版信息
Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1222-6. doi: 10.1107/S0907444905018834. Epub 2005 Aug 16.
The X-ray structure of the enzyme 5-aminolaevulinic acid dehydratase (ALAD) from yeast complexed with the competitive inhibitor 5-hydroxylaevulinic acid has been determined at a resolution of 1.9 A. The structure shows that the inhibitor is bound by a Schiff-base link to one of the invariant active-site lysine residues (Lys263). The inhibitor appears to bind in two well defined conformations and the interactions made by it suggest that it is a very close analogue of the substrate 5-aminolaevulinic acid (ALA).
已测定酵母中与竞争性抑制剂5-羟基乙酰丙酸复合的5-氨基乙酰丙酸脱水酶（ALAD）的X射线结构，分辨率为1.9埃。该结构表明，抑制剂通过席夫碱连接与一个不变的活性位点赖氨酸残基（Lys263）结合。抑制剂似乎以两种明确的构象结合，其形成的相互作用表明它是底物5-氨基乙酰丙酸（ALA）的非常相似的类似物。
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