scholarly journals Identification and Characterization of a DmoB Flavin Oxidoreductase from a Putative Two-Component DMS C-Monooxygenase

ACS Omega ◽  
2020 ◽  
Vol 5 (17) ◽  
pp. 9830-9838
Author(s):  
D. Scott Hammers ◽  
Caroline M. Donaghy ◽  
Sarah L. Heiss ◽  
Lydia M. Harris ◽  
Jackson M. Gordon ◽  
...  
2019 ◽  
Vol 38 (6) ◽  
pp. 683-692
Author(s):  
Baohua Chen ◽  
Tingting Zou ◽  
Long Zou ◽  
Haiyan Ni ◽  
Yunhong Huang ◽  
...  

2003 ◽  
Vol 218 (1) ◽  
pp. 121-126 ◽  
Author(s):  
Yi-Chyi Lai ◽  
Ging-Ting Lin ◽  
Shu-Li Yang ◽  
Hwan-You Chang ◽  
Hwei-Ling Peng

2011 ◽  
Vol 10 (10) ◽  
pp. 1370-1374 ◽  
Author(s):  
Chirayu Desai ◽  
John Mavrianos ◽  
Neeraj Chauhan

ABSTRACT We report here the identification and characterization of a previously uncharacterized, two-component response regulator gene (orf19.5843) from Candida albicans . Because of its apparent functions in stress adaptation, we have named this gene SRR1 ( s tress r esponse r egulator 1). Disruption of SRR1 causes defects in hyphal development, reduced resistance to stress, and severe virulence attenuation in the mouse model of disseminated candidiasis.


2007 ◽  
Vol 189 (23) ◽  
pp. 8556-8563 ◽  
Author(s):  
Jung-Kul Lee ◽  
Huimin Zhao

ABSTRACT Two-component oxygenases catalyze a wide variety of important oxidation reactions. Recently we characterized a novel arylamine N-oxygenase (PrnD), a new member of the two-component oxygenase family (J. Lee et al., J. Biol. Chem. 280:36719-36728, 2005). Although arylamine N-oxygenases are widespread in nature, aminopyrrolnitrin N-oxygenase (PrnD) represents the only biochemically and mechanistically characterized arylamine N-oxygenase to date. Here we report the use of bioinformatic and biochemical tools to identify and characterize the reductase component (PrnF) involved in the PrnD-catalyzed unusual arylamine oxidation. The prnF gene was identified via sequence analysis of the whole genome of Pseudomonas fluorescens Pf-5 and subsequently cloned and overexpressed in Escherichia coli. The purified PrnF protein catalyzes reduction of flavin adenine dinucleotide (FAD) by NADH with a k cat of 65 s−1 (K m = 3.2 μM for FAD and 43.1 μM for NADH) and supplies reduced FAD to the PrnD oxygenase component. Unlike other known reductases in two-component oxygenase systems, PrnF strictly requires NADH as an electron donor to reduce FAD and requires unusual protein-protein interaction with the PrnD component for the efficient transfer of reduced FAD. This PrnF enzyme represents the first cloned and characterized flavin reductase component in a novel two-component arylamine oxygenase system.


Sign in / Sign up

Export Citation Format

Share Document