Molecular insights into substrate specificity of Rhodococcus ruber CGMCC3090 by gene cloning and homology modeling.

Abstract:

:The primary aim of this study was to decipher the catalytic functions of the NHase with wide substrate spectra from Rhodococcus ruber CGMCC3090 by computer modeling and substrate docking. 3D structure model of the enzyme was built by computer modeling to obtain the optimal structure. The larger binding site cavity (559 Å(3)) indicated that this NHase may catalyze a large variety of substrates of nitriles. Some key residues such as αGlu82, αGln83, βTyr71, β Tyr72, β Arg52 and β Arg55 surrounding the binding site were unique compared with those of 3QXE as a template, indicating that the enzyme may have unusual substrate specificity. The docking and the biotransformation experiments demonstrated that the special docking pose and shorter distance proved to be more effective for the enzyme to improve function.

journal_name

Enzyme Microb Technol

authors

Wang S,Dai Y,Wang J,Shen Y,Zhai Y,Zheng H,Wang M

doi

10.1016/j.enzmictec.2012.11.004

subject

Has Abstract

pub_date

2013-02-05 00:00:00

pages

111-7

issue

2

eissn

0141-0229

issn

1879-0909

pii

S0141-0229(12)00183-4

journal_volume

52

pub_type

杂志文章