Crystal structure of nitrile hydratase from a thermophilic Bacillus smithii

被引：54

作者：

Hourai, S ^{[1
]}

Miki, M ^{[1
]}

Takashima, Y ^{[1
]}

Mitsuda, S ^{[1
]}

Yanagi, K ^{[1
]}

机构：

[1] Sumitomo Chem Co Ltd, Environm Hlth Sci Lab, Osaka 5548558, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2003年 / 312卷 / 02期

关键词：

NHase; Bacillus smithii;

D O I：

10.1016/j.bbrc.2003.10.124

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：340 / 345

页数：6

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