NDLI: Active site modifications in pentaerythritol tetranitrate reductase can lead to improved product enantiopurity, decreased by-product formation and altered stereochemical outcome in reactions with α,β-unsaturated nitroolefins

Please wait, while we are loading the content...

Active site modifications in pentaerythritol tetranitrate reductase can lead to improved product enantiopurity, decreased by-product formation and altered stereochemical outcome in reactions with α,β-unsaturated nitroolefins

Interaction of ethene and ethyne with bare and hydrogenated Ir₄ clusters. A density functional study

Synthetic strategy for Fe-MCM-41 catalyst: a key factor for homogeneous or heterogeneous phenol oxidation

Design of silver(i)-heteropolyacids: toward the molecular control of reactivity in organic chemistry

Oxidative dehydrogenation of propane using lattice oxygen of vanadium oxides on silica

NiO microspheres with tunable porosity and morphology effects for CO oxidation

Catalytic performance of La_1−xEr_xCoO₃ perovskite for the deoxidization of coal bed methane and role of erbium in a catalyst

Support effects on the structure and performance of ruthenium catalysts for the Fischer–Tropsch synthesis

Structure and catalytic properties of hexagonal molybdenum disulfide nanoplates

Carbon dioxide reforming of methane over ordered mesoporous NiO–Al₂O₃ composite oxides

Kinetic studies and modelling of the production of fructooligosaccharides by fructosyltransferase from Rhodotorula sp

A versatile supported cobalt(ii) complex for heterogeneously catalysed processes: conventional vs. microwave irradiation protocols

Nature of vanadium species on vanadium silicalite-1 zeolite and their stability in hydroxylation reaction of benzene to phenol

A new method to obtain β-glucan from Saccharomyces cerevisiae cells

Catalytic performance and mechanism of KF-loaded catalysts for biodiesel synthesis

Back cover

Catalysis Science & Technology Vol - 1 Issue - 5

Catalysis Science & Technology Vol - 1 Issue - 4

Catalysis Science & Technology Vol - 1 Issue - 3

Catalysis Science & Technology Vol - 1 Issue - 2

Catalysis Science & Technology Vol - 1 Issue - 1

Active site modifications in pentaerythritol tetranitrate reductase can lead to improved product enantiopurity, decreased by-product formation and altered stereochemical outcome in reactions with α,β-unsaturated nitroolefins

Content Provider	Royal Society of Chemistry (RSC)
Author	Sakuma, Michiyo Scrutton, Nigel S. Fryszkowska, Anna Gardiner, John M. Stephens, Gill M. Toogood, Helen
Copyright Year	2011
Abstract	This work describes a site-directed mutagenesis study of pentaerythritol tetranitrate reductase (PETN reductase) to probe the role of key active site residues in influencing both product enantiopurity and the ratio of CC vs. nitro-group reduction with 2-phenyl-1-nitropropene. Comparative biotransformations of wild type and single/double mutants of PETN reductase with 2-phenyl-1-nitropropene showed that one enzyme scaffold was capable of generating both enantiomeric products with improved enantiopurities by a manipulation of the reaction conditions and/or the presence of a one or two key mutations. These changes located at key active site residues were sufficient to moderately improve product enantiopurity, cause a switch in the major product enantiomer formed and/or promote or eliminate side-product formation. The mutation of substrate-binding residue Y351 to alanine and phenylalanine improved the biocatalytic potential of PETN reductase by the elimination of a competing side reaction. The crystal structures of three mutants at residue Y351 (PDB codes: 3P81, 3P84 and 3P8J) show that only subtle changes in the active site environment may be necessary to generate significantly improved biocatalysts.
Starting Page	948
Ending Page	957
Page Count	10
File Format	HTM / HTML PDF
ISSN	20444753
Volume Number	1
Issue Number	6
Journal	Catalysis Science & Technology
DOI	10.1039/c0cy00092b
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Nitro compound Alanine Phenylalanine Enzyme Site-directed mutagenesis Active site Enantiomer Pentaerythritol tetranitrate Phenyl group Mutation Protein Data Bank
Content Type	Text
Resource Type	Article
Subject	Catalysis

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Structure-Based Insight into the Asymmetric Bioreduction of the CC Double Bond of α,β-Unsaturated Nitroalkenes by Pentaerythritol Tetranitrate Reductase

Structure-Based Insight into the Asymmetric Bioreduction of the C=C Double Bond of α,β-Unsaturated Nitroalkenes by Pentaerythritol Tetranitrate Reductase

Electro-enzymatic viologen-mediated substrate reduction using pentaerythritol tetranitrate reductase and a parallel, segmented fluid flow system

Hypervalent Iodine Oxidation of α, β-Unsaturated Carbonyl Compounds

l.2.3 Reactions of α,β-Unsaturated Carbonyl Compounds

Kinetic and mechanistic studies of morphinone reductase and pentaerythritol tetranitrate reductase

1H, 15N and 13C backbone resonance assignments of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2

Bipartite recognition and conformational sampling mechanisms for hydride transfer from nicotinamide coenzyme to FMN in pentaerythritol tetranitrate reductase

Cu(NO$_{3}$)$_{2}$-catalyzed nitrodecarboxylation of α,β-unsaturated acids: facile synthesis of (E)-nitroolefins under additive-free conditions

Active site modifications in pentaerythritol tetranitrate reductase can lead to improved product enantiopurity, decreased by-product formation and altered stereochemical outcome in reactions with α,β-unsaturated nitroolefins

Similar Documents

Structure-Based Insight into the Asymmetric Bioreduction of the CC Double Bond of α,β-Unsaturated Nitroalkenes by Pentaerythritol Tetranitrate Reductase

Structure-Based Insight into the Asymmetric Bioreduction of the C=C Double Bond of α,β-Unsaturated Nitroalkenes by Pentaerythritol Tetranitrate Reductase

Electro-enzymatic viologen-mediated substrate reduction using pentaerythritol tetranitrate reductase and a parallel, segmented fluid flow system

Hypervalent Iodine Oxidation of α, β-Unsaturated Carbonyl Compounds

l.2.3 Reactions of α,β-Unsaturated Carbonyl Compounds

Kinetic and mechanistic studies of morphinone reductase and pentaerythritol tetranitrate reductase

1H, 15N and 13C backbone resonance assignments of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2

Bipartite recognition and conformational sampling mechanisms for hydride transfer from nicotinamide coenzyme to FMN in pentaerythritol tetranitrate reductase

Cu(NO$_{3}$)$_{2}$-catalyzed nitrodecarboxylation of α,β-unsaturated acids: facile synthesis of (E)-nitroolefins under additive-free conditions

Active site modifications in pentaerythritol tetranitrate reductase can lead to improved product enantiopurity, decreased by-product formation and altered stereochemical outcome in reactions with α,β-unsaturated nitroolefins