Crystal structure of nitrile hydratase from a thermophilic Bacillus smithii
Crystal structure of nitrile hydratase from a thermophilic Bacillus smithii
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DOI：
10.1016/j.bbrc.2003.10.124
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发表时间：
2003-12-12
影响因子：
3.1
通讯作者：
Yanagi, K
中科院分区：
文献类型：
--
作者：
Hourai, S;Miki, M;Yanagi, K
测定了来自史氏芽孢杆菌SC-J 05 -1的腈水合酶（NHase）的晶体结构。我们的结构分析表明，一些残基，似乎是负责底物识别是不同的其他NHases。特别地，来自B的NHase的β亚基中的Phe 52。Smithii像小盖子一样部分地覆盖金属中心，并使活性部位裂缝变窄。众所周知，来自B. Smithii特别喜欢脂肪族腈作为其底物，而不是芳香族腈，我们现在可以推断Phe 52残基可能在该酶的底物特异性中起关键作用。这一发现使我们认为这些残基的取代可能改变酶的底物特异性。(C)2003年爱思唯尔公司All rights reserved.
The crystal structure of the nitrile hydratase (NHase) from Bacillus smithii SC-J05-1 was determined. Our analysis of the structure shows that some residues that seem to be responsible for substrate recognition are different from those of other NHases. In particular, the Phe52 in the beta subunit of NHase from B. smithii covers the metal center partially like a small lid and narrows the active site cleft. It is well known that the NHase from B. smithii especially prefers aliphatic nitriles for its substrate rather than aromatic ones, and we can now infer that the Phe52 residue may play a key role in the substrate specificity for this enzyme. this finding leads us to suggest that substitution of these residues may alter the substrate specificity of the enzyme. (C) 2003 Elsevier Inc. All rights reserved.