Novel catalytic activity of nitrile hydratase from Rhodococcus sp. N771

2008 ◽  
Vol 106 (2) ◽  
pp. 174-179 ◽  
Author(s):  
Kayoko Taniguchi ◽  
Kensuke Murata ◽  
Yoshihiko Murakami ◽  
Shunya Takahashi ◽  
Takemichi Nakamura ◽  
...  
1991 ◽  
Vol 146 (2) ◽  
pp. 89-98 ◽  
Author(s):  
M.R. Kaakeh ◽  
J.-L. Legras ◽  
R. Duran ◽  
Ch.K.N. Chan Kwo Chion ◽  
A. Arnaud ◽  
...  

Author(s):  
Zhongyi Cheng ◽  
Weimiao Zhang ◽  
Yuanyuan Xia ◽  
Dong Ma ◽  
Zhe-Min Zhou

The βGlu50 residue located adjacent to the substrate access tunnel entrance of nitrile hydratase from Pseudonocardia thermophila JCM3095 acts as an anchoring residue. Breaking the salt bridge between β50 residue...


1992 ◽  
Vol 672 (1 Enzyme Engine) ◽  
pp. 29-36 ◽  
Author(s):  
JUN HONDA ◽  
TERUYUKI NAGAMUNE ◽  
YOSHITAKA TERATANI ◽  
AKIRA HIRATA ◽  
HIROYUKI SASABE ◽  
...  

Molecules ◽  
2020 ◽  
Vol 25 (20) ◽  
pp. 4806
Author(s):  
Zhongyi Cheng ◽  
Yao Lan ◽  
Junling Guo ◽  
Dong Ma ◽  
Shijin Jiang ◽  
...  

High thermostability and catalytic activity are key properties for nitrile hydratase (NHase, EC 4.2.1.84) as a well-industrialized catalyst. In this study, rational design was applied to tailor the thermostability of NHase from Pseudonocardia thermophila JCM3095 (PtNHase) by combining FireProt server prediction and molecular dynamics (MD) simulation. Site-directed mutagenesis of non-catalytic residues provided by the rational design was subsequentially performed. The positive multiple-point mutant, namely, M10 (αI5P/αT18Y/αQ31L/αD92H/βA20P/βP38L/βF118W/βS130Y/βC189N/βC218V), was obtained and further analyzed. The Melting temperature (Tm) of the M10 mutant showed an increase by 3.2 °C and a substantial increase in residual activity of the enzyme at elevated temperatures was also observed. Moreover, the M10 mutant also showed a 2.1-fold increase in catalytic activity compared with the wild-type PtNHase. Molecular docking and MD simulations demonstrated better substrate affinity and improved thermostability for the mutant.


2000 ◽  
Vol 9 (5) ◽  
pp. 1024-1030 ◽  
Author(s):  
Taku Murakami ◽  
Masaki Nojiri ◽  
Hiroshi Nakayama ◽  
Naoshi Dohmae ◽  
Koji Takio ◽  
...  

2018 ◽  
Vol 6 (6) ◽  
pp. e01526-17 ◽  
Author(s):  
Andrey D. Novikov ◽  
Konstantin V. Lavrov ◽  
Artem S. Kasianov ◽  
Tatyana V. Gerasimova ◽  
Alexander S. Yanenko

ABSTRACT Rhodococcus sp. strain M8 is a nitrile-degrading bacterium isolated from acrylonitrile-contaminated sites. This strain produces the enzymes for sequential nitrile degradation, cobalt-type nitrile hydratase, and amidase in large amounts. Its draft genome sequence, announced here, has an estimated size of 6.3 Mbp.


1991 ◽  
Vol 220 (2) ◽  
pp. 221-222 ◽  
Author(s):  
Teruyuki Nagamune ◽  
Jun Honda ◽  
Won-Dai Cho ◽  
Nobuo Kamiya ◽  
Yoshitaka Teratani ◽  
...  

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