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

Paper ID Volume ID Publish Year Pages File Format Full-Text
17083 42639 2013 7 PDF Available
Title
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 Å3) 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.

Graphical abstract.Figure optionsDownload full-size imageDownload as PowerPoint slideHighlights► The 3-D structure model of NHase from R. ruber CGMCC3090 was built. ► The NHase with larger binding site cavity may catalyze a large variety of nitriles. ► The NHase had a preference for mono-nitriles rather than dinitriles. ► The studies provide experimental supports for enunciating the NHase functions.

Keywords
Rhodococcus ruber; NHase; Structure; Function; Homology modeling; Docking
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Molecular insights into substrate specificity of Rhodococcus ruber CGMCC3090 by gene cloning and homology modeling
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 52, Issue 2, 5 February 2013, Pages 111–117
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us