Substrate Specificity Engineering of β-Mannosidase and β-Glucosidase fromPyrococcusby Exchange of Unique Active Site Residues†

Biochemistry ◽  
2002 ◽  
Vol 41 (12) ◽  
pp. 4147-4155 ◽  
Author(s):  
Thijs Kaper ◽  
Hester H. van Heusden ◽  
Bert van Loo ◽  
Andrea Vasella ◽  
John van der Oost ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Active Site ◽  
Active Site Residues

scholarly journals Redesigning the Substrate Specificity of an Enzyme by Cumulative Effects of the Mutations of Non-active Site Residues

1999 ◽  
Vol 274 (4) ◽  
pp. 2344-2349 ◽  
Author(s):  
Shinya Oue ◽  
Akihiro Okamoto ◽  
Takato Yano ◽  
Hiroyuki Kagamiyama
Keyword(s):  
Substrate Specificity ◽  
Active Site ◽  
Cumulative Effects ◽  
Active Site Residues

scholarly journals Mechanism of the Flavoprotein d-6-Hydroxynicotine Oxidase: Substrate Specificity, pH and Solvent Isotope Effects, and Roles of Key Active-Site Residues

Biochemistry ◽  
2019 ◽  
Vol 58 (21) ◽  
pp. 2534-2541
Author(s):  
Paul F. Fitzpatrick ◽  
Vi Dougherty ◽  
Bishnu Subedi ◽  
Jesus Quilantan ◽  
Cynthia S. Hinck ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Active Site ◽  
Isotope Effects ◽  
Active Site Residues ◽  
Solvent Isotope ◽  
Solvent Isotope Effects

Role of active-site residues Tyr55 and Tyr114 in catalysis and substrate specificity ofCorynebacterium diphtheriaeC-S lyase

2014 ◽  
Vol 83 (1) ◽  
pp. 78-90 ◽  
Author(s):  
Alessandra Astegno ◽  
Alessandra Allegrini ◽  
Stefano Piccoli ◽  
Alejandro Giorgetti ◽  
Paola Dominici
Keyword(s):  
Substrate Specificity ◽  
Active Site ◽  
Active Site Residues

Active site residues controlling substrate specificity in 2-nitrotoluene dioxygenase from Acidovorax sp. strain JS42

2005 ◽  
Vol 32 (10) ◽  
pp. 465-473 ◽  
Author(s):  
Kyung-Seon Lee ◽  
Juanito V. Parales ◽  
Rosmarie Friemann ◽  
Rebecca E. Parales
Keyword(s):  
Substrate Specificity ◽  
Active Site ◽  
Active Site Residues

scholarly journals Genome Mining, Phylogenetic and Structural Analysis of Bacterial Nitrilases for the Biodegradation of Nitrile Compounds

2021 ◽  
Author(s):  
Richa Salwan ◽  
Vivek Sharma ◽  
Surajit Das
Keyword(s):  
Structural Analysis ◽  
Substrate Specificity ◽  
Active Site ◽  
Structural Information ◽  
Genome Mining ◽  
Binding Pocket ◽  
Catalytic Triad ◽  
Vital Role ◽  
Active Site Residues ◽  
Motif Analysis

Abstract Microbial nitrilases play vital role in biodegradation of nitrile-containing contaminants in pollutant and effluents treatments in chemical and textile industries as well as the biosynthesis of IAA from tryptophan in plants. However, the lack of structural information hinders the correlation of its activity and substrate specificity. Here, we have identified bacterial genomes for nitrilases bearing unassigned functions including hypothetical, uncharacterized, or putative role. The genomic annotations revealed four predicted nitrilases encoding genes as uncharacterized subgroup of the nitrilase superfamily. Further, the annotation of these nitrilases revealed relatedness with nitrilase hydratases and cyanoalanine hydratases. The characterization of motif analysis of these protein sequences, predicted a single motif of 20-28 aa, and glutamate (E), lysine (K) and cysteine (C) residues as a part of catalytic triad along with several active site residues. The structural analysis of the modeled nitrilases revealed geometrical and close conformation of α-helices and β-sheets arranged in a sandwich structure. The catalytic residues constituted the substrate binding pocket and exhibited the wide nitrile substrate spectra for both aromatic and aliphatic nitriles containing compounds. The aromatic amino acid residues Y159 in active site were predicted to show importance for substrate specificity. The substitution of non-aromatic alanine residue in place of Y159 completely disrupted the catalytic activity for indole-3-acetonitrile. The present study reports several uncharacterized nitrilases which have not been reported so far for their role in the biodegradation of pollutants, xenobiotics which could find applications in industries.

Modification of Near Active Site Residues in Organophosphorus Hydrolase Reduces Metal Stoichiometry and Alters Substrate Specificity†

Biochemistry ◽  
1999 ◽  
Vol 38 (10) ◽  
pp. 2866-2872 ◽  
Author(s):  
Barbara diSioudi ◽  
Janet K. Grimsley ◽  
Kaihua Lai ◽  
James R. Wild
Keyword(s):  
Substrate Specificity ◽  
Active Site ◽  
Organophosphorus Hydrolase ◽  
Active Site Residues
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