An anchoring residue adjacent to the substrate access tunnel entrance of nitrile hydratase directs its catalytic activity towards 3-cyanopyridine

2021 ◽  
Author(s):  
Zhongyi Cheng ◽  
Weimiao Zhang ◽  
Yuanyuan Xia ◽  
Dong Ma ◽  
Zhe-Min Zhou
Keyword(s):  
Catalytic Activity ◽  
Nitrile Hydratase ◽  
Salt Bridge ◽  
Tunnel Entrance

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...

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 ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Nitrile Hydratase ◽  
Rhodococcus Sp

scholarly journals Computational Design of Nitrile Hydratase from Pseudonocardia thermophila JCM3095 for Improved Thermostability

Molecules ◽  
2020 ◽  
Vol 25 (20) ◽  
pp. 4806
Author(s):  
Zhongyi Cheng ◽  
Yao Lan ◽  
Junling Guo ◽  
Dong Ma ◽  
Shijin Jiang ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Rational Design ◽  
Nitrile Hydratase ◽  
Elevated Temperatures ◽  
Residual Activity ◽  
Fold Increase ◽  
Computational Design ◽  
Site Directed Mutagenesis ◽  
Multiple Point ◽  
Substrate Affinity

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.

scholarly journals Post-translational modification is essential for catalytic activity of nitrile hydratase

2000 ◽  
Vol 9 (5) ◽  
pp. 1024-1030 ◽  
Author(s):  
Taku Murakami ◽  
Masaki Nojiri ◽  
Hiroshi Nakayama ◽  
Naoshi Dohmae ◽  
Koji Takio ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Nitrile Hydratase ◽  
Post Translational Modification

Insights into stabilizing interactions in the distorted domain-swapped dimer ofSalmonella typhimuriumsurvival protein

2015 ◽  
Vol 71 (9) ◽  
pp. 1812-1823 ◽  
Author(s):  
Yamuna Kalyani Mathiharan ◽  
H. S. Savithri ◽  
M. R. N. Murthy
Keyword(s):  
Hydrogen Bond ◽  
Catalytic Activity ◽  
Salt Bridge ◽  
Salt Bridges ◽  
X Ray ◽  
Dimeric Interface ◽  
Distorted Structure ◽  
Dimeric Protein ◽  
The Stability

The survival protein SurE fromSalmonella typhimurium(StSurE) is a dimeric protein that functions as a phosphatase. SurE dimers are formed by the swapping of a loop with a pair of β-strands and a C-terminal helix between two protomers. In a previous study, the Asp230 and His234 residues were mutated to Ala to abolish a hydrogen bond that was thought to be crucial for C-terminal helix swapping. These mutations led to functionally inactive and distorted dimers in which the two protomers were related by a rotation of 167°. New salt bridges involving Glu112 were observed in the dimeric interface of the H234A and D230A/H234A mutants. To explore the role of these salt bridges in the stability of the distorted structure, E112A, E112A/D230A, E112A/H234A, E112A/D230A/H234A, R179L/H180A/H234A and E112A/R179L/H180A/H234A mutants were constructed. X-ray crystal structures of the E112A, E112A/H234A and E112A/D230A mutants could be determined. The dimeric structures of the E112A and E112A/H234A mutants were similar to that of native SurE, while the E112A/D230A mutant had a residual rotation of 11° between theBchains upon superposition of theAchains of the mutant and native dimers. The native dimeric structure was nearly restored in the E112A/H234A mutant, suggesting that the new salt bridge observed in the H234A and D230A/H234A mutants was indeed responsible for the stability of their distorted structures. Catalytic activity was also restored in these mutants, implying that appropriate dimeric organization is necessary for the activity of SurE.

scholarly journals The Alpha Subunit of Nitrile Hydratase Is Sufficient for Catalytic Activity and Post-Translational Modification

Biochemistry ◽  
2014 ◽  
Vol 53 (24) ◽  
pp. 3990-3994 ◽  
Author(s):  
Micah T. Nelp ◽  
Andrei V. Astashkin ◽  
Linda A. Breci ◽  
Reid M. McCarty ◽  
Vahe Bandarian
Keyword(s):  
Catalytic Activity ◽  
Nitrile Hydratase ◽  
Alpha Subunit ◽  
Post Translational Modification

scholarly journals Evidence of the Participation of Remote Residues in the Catalytic Activity of Co-Type Nitrile Hydratase fromPseudomonas putida

Biochemistry ◽  
2011 ◽  
Vol 50 (22) ◽  
pp. 4923-4935 ◽  
Author(s):  
Heather R. Brodkin ◽  
Walter R. P. Novak ◽  
Amy C. Milne ◽  
J. Alejandro D’Aquino ◽  
N. M. Karabacak ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Nitrile Hydratase ◽  
Remote Residues

scholarly journals A single intersubunit salt bridge affects oligomerization and catalytic activity in a bacterial quinone reductase

FEBS Journal ◽  
2009 ◽  
Vol 276 (18) ◽  
pp. 5263-5274 ◽  
Author(s):  
Alexandra Binter ◽  
Nicole Staunig ◽  
Ilian Jelesarov ◽  
Karl Lohner ◽  
Bruce A. Palfey ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Salt Bridge ◽  
Quinone Reductase
Sign in / Sign up

Export Citation Format

Share Document