Reaction mechanism of azoreductases suggests convergent evolution with quinone oxidoreductases

Ryan, Ali; Wang, Chan-Ju; Laurieri, Nicola; Westwood, Isaac M.; Sim, Edith

doi:10.1007/s13238-010-0090-2

Cited by 56 publications

(40 citation statements)

References 53 publications

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“…In previous reports, the substrate recognitions of respective azoreductases including azo dyes, nitro-aromatic compounds, and quinones have been determined (Zimmermann et al 1982;Liu et al 2008;Ryan et al 2010b). A broad substrate specificities of azoreductases were reported from alkaliphilic Bacillus badius, Aquiflexum sp., and neutrophilic Lysinibacillus sphaericus against a range of azo dyes and nitro compounds (Misal et al 2011(Misal et al , 2013(Misal et al , 2014(Misal et al , 2015.…”

Section: Kinetic Properties and Substrate Specificities Of Azoreductasesmentioning

confidence: 99%

Azoreductase: a key player of xenobiotic metabolism

Misal

Gawai

2018

Bioresour. Bioprocess.

142

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Azoreductases are diverse flavoenzymes widely present among microorganisms and higher eukaryotes. They are mainly involved in the biotransformation and detoxification of azo dyes, nitro-aromatic, and azoic drugs. Reduction of azo bond and reductive activation of pro-drugs at initial level is a crucial stage in degradation and detoxification mechanisms. Using azoreductase-based microbial enzyme systems that are biologically accepted and ecofriendly demonstrated complete degradation of azo dyes. Azoreductases are flavin-containing or flavin-free group of enzymes, utilizing the nicotinamide adenine dinucleotide or nicotinamide adenine dinucleotide phosphate as a reducing equivalent. Azoreductases from anaerobic microorganisms are highly oxygen sensitive, while azoreductases from aerobic microorganisms are usually oxygen insensitive. They have variable pH, temperature stability, and wide substrate specificity. Azo dyes, nitro-aromatic compounds, and quinones are the known substrates of azoreductase. The present review gives an overview of recent developments in the known azoreductase enzymes from different microorganisms, its novel classification scheme, significant characteristics, and their plausible degradation mechanisms.

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Section: Kinetic Properties and Substrate Specificities Of Azoreductasesmentioning

confidence: 99%

Azoreductase: a key player of xenobiotic metabolism

Misal

Gawai

2018

Bioresour. Bioprocess.

142

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“…Convergent evolution of azoreductases and quinone reductases has been proposed based on similar reaction mechanisms involving the flavin-mediated reduction of an organic molecule with NAD(P)H and substrate scope (37,38). The lack of enzymatic activity with the azo dye methyl red indicates that PA1024 is not an azoreductase.…”

Section: Exx(t//s)xlhxrxhxn(t/s)xr(v/i)mentioning

confidence: 99%

Functional Annotation of a Presumed Nitronate Monoxygenase Reveals a New Class of NADH:Quinone Reductases

Ball¹,

Salvi²,

Gadda³

2016

Journal of Biological Chemistry

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The protein PA1024 from Pseudomonas aeruginosa PAO1 is currently classified as 2-nitropropane dioxygenase, the previous name for nitronate monooxygenase in the GenBank TM and PDB databases, but the enzyme was not kinetically characterized. In this study, PA1024 was purified to high levels, and the enzymatic activity was investigated by spectroscopic and polarographic techniques. Purified PA1024 did not exhibit nitronate monooxygenase activity; however, it displayed NADH:quinone reductase and a small NADH:oxidase activity. The enzyme preferred NADH to NADPH as a reducing substrate. PA1024 could reduce a broad spectrum of quinone substrates via a Ping Pong Bi Bi steady-state kinetic mechanism, generating the corresponding hydroquinones. The reductive half-reaction with NADH showed a k red value of 24 s ؊1 and an apparent K d value estimated in the low micromolar range. The enzyme was not able to reduce the azo dye methyl red, routinely used in the kinetic characterization of azoreductases. Finally, we revisited and modified the existing six conserved motifs of PA1024, which define a new class of NADH:quinone reductases and are present in more than 490 hypothetical proteins in the GenBank TM , the vast majority of which are currently misannotated as nitronate monooxygenase.

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“…UV/Vis spectra were collected for each of the expressed azoreductases (Sup Fig 4). paWrbA lacked the characteristic flavin absorption peaks found in other azoreductases [13]. The peaks were present in all of the other proteins but were not as well defined as one would expect.…”

Section: Flavin Cofactor Selectivitymentioning

confidence: 84%

“…One of the reasons for the lack of understanding of the physiological role of this enzyme family is that in addition to azo compounds (Sup Fig 1) they reduce a broad range of substrates, including quinones [13] and nitrofurans [14]. As a result of their azoreductase activity much research has focused on the identification of azoreductases for the bioremediation of azo dye containing waste waters [15,16] and engineering of these enzymes for this purpose [17].…”

Section: Introductionmentioning

confidence: 99%

“…Mechanistic studies identified a common mechanism for the reduction of azo and quinone substrates [13,19] and led to the proposition that azoreductases (EC: 1.7.1.6) and NAD(P)H quinone oxidoreductases (EC: 1.6.99.2) are members of a single superfamily [1]. One of the reasons these two functional classes were kept separate is the sequence diversity among the members.…”

Section: Introductionmentioning

confidence: 99%

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Identification of novel members of the bacterial azoreductase family in Pseudomonas aeruginosa

Crescente

Holland

Kashyap

et al. 2016

Biochemical Journal

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Abstract:Azoreductases are a family of diverse enzymes found in many pathogenic bacteria as well as distant homologues being present in eukarya. In addition to having azoreductase activity these enzymes are also suggested to have NAD(P)H quinone oxidoreductase activity which leads to a proposed role in plant pathogenesis. Azoreductases have also been suggested to play role in the mammalian pathogenesis of Pseudomonas aeruginosa. In view of the importance of P. aeruginosa as a pathogen, we therefore characterised recombinant enzymes following expression of a group of putative azoreductase genes from P. aeruginosa expressed in Escherichia coli. The enzymes include members of the "Arsenic resistance protein H" (ArsH), "tryptophan repressor binding protein A" (WrbA), "modulator of drug activity B" (MdaB) and YieF families. The ArsH, MdaB and YieF family members all show azoreductase and NAD(P)H quinone oxidoreductase activities. In contrast, WrbA is the first enzyme to show NAD(P)H quinone oxidoreductase activity but does not reduce any of the 11 azo compounds tested under a wide range of conditions. These studies will allow further investigation of the possible role of these enzymes in the pathogenesis of P. aeruginosa.

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Reaction mechanism of azoreductases suggests convergent evolution with quinone oxidoreductases

Cited by 56 publications

References 53 publications

Azoreductase: a key player of xenobiotic metabolism

Azoreductase: a key player of xenobiotic metabolism

Functional Annotation of a Presumed Nitronate Monoxygenase Reveals a New Class of NADH:Quinone Reductases

Identification of novel members of the bacterial azoreductase family in Pseudomonas aeruginosa

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