Imperial College London
Alternate

DrJohnHeap

Faculty of Natural Sciences, Department of Life Sciences

Honorary Senior Lecturer
 
 
 
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Contact

 

+44 (0)20 7594 5355j.heap

 
 
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Location

 

Bessemer BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Sellés:2018:10.1016/j.bbapap.2017.11.005,
author = {Sellés, Vidal L and Kelly, CL and Mordaka, PM and Heap, JT},
doi = {10.1016/j.bbapap.2017.11.005},
journal = {Biochim Biophys Acta Proteins Proteom},
pages = {327--347},
title = {Review of NAD(P)H-dependent oxidoreductases: Properties, engineering and application.},
url = {http://dx.doi.org/10.1016/j.bbapap.2017.11.005},
volume = {1866},
year = {2018}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - NAD(P)H-dependent oxidoreductases catalyze the reduction or oxidation of a substrate coupled to the oxidation or reduction, respectively, of a nicotinamide adenine dinucleotide cofactor NAD(P)H or NAD(P)+. NAD(P)H-dependent oxidoreductases catalyze a large variety of reactions and play a pivotal role in many central metabolic pathways. Due to the high activity, regiospecificity and stereospecificity with which they catalyze redox reactions, they have been used as key components in a wide range of applications, including substrate utilization, the synthesis of chemicals, biodegradation and detoxification. There is great interest in tailoring NAD(P)H-dependent oxidoreductases to make them more suitable for particular applications. Here, we review the main properties and classes of NAD(P)H-dependent oxidoreductases, the types of reactions they catalyze, some of the main protein engineering techniques used to modify their properties and some interesting examples of their modification and application.
AU  - Sellés,Vidal L
AU  - Kelly,CL
AU  - Mordaka,PM
AU  - Heap,JT
DO  - 10.1016/j.bbapap.2017.11.005
EP  - 347
PY  - 2018///
SN  - 1570-9639
SP  - 327
TI  - Review of NAD(P)H-dependent oxidoreductases: Properties, engineering and application.
T2  - Biochim Biophys Acta Proteins Proteom
UR  - http://dx.doi.org/10.1016/j.bbapap.2017.11.005
UR  - https://www.ncbi.nlm.nih.gov/pubmed/29129662
UR  - http://hdl.handle.net/10044/1/53944
VL  - 1866
ER  -
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