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Cofactor promiscuity among F 420 -dependent reductases enables them to catalyse both oxidation and reduction of the same substrate

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Date

2012

Authors

Lapalikar, Gauri V
Taylor, Matthew C
Warden, Andrew C
Onagi, Hideki
Hennessy, James E
Mulder, Roger J
Scott, Colin
Brown, Susan E
Russell, Robyn J
Easton, Christopher

Journal Title

Journal ISSN

Volume Title

Publisher

Royal Society of Chemistry

Abstract

The recently reported F420H2-dependent reductases (FDRs) catalyse the reduction of aflatoxins and coumarin via hydrogenation of the α,β-unsaturated moiety. We report that three FDRs (MSMEG-2027, MSMEG-6848 and MSMEG-3356) from Mycobacterium smegmatis al

Description

Keywords

Keywords: Catalyse; Catalytic functions; Cofactors; Mycobacterium smegmatis; Oxidation and reduction; Structural isomers; Bacteria; Catalysis; Enzymes; Isomers; Oxidation; Aflatoxins

Citation

URI

http://hdl.handle.net/1885/61579

Collections

ANU Research Publications

Source

Catalysis Science and Technology

Type

Journal article

Book Title

Entity type

Access Statement

License Rights

DOI

10.1039/c2cy20129a

Restricted until

2037-12-31

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Description
01_Lapalikar_Cofactor_promiscuity_among_F_2012.pdf (2.92 MB)

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