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Volume 12
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10.21775/cimb.012.043
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Current Issues in Molecular Biology is published by MDPI from Volume 43 Issue 1 (2021). Previous articles were published by another publisher in Open Access under a CC-BY (or CC-BY-NC-ND) licence, and they are hosted by MDPI on mdpi.com as a courtesy and upon agreement with Caister Press.
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Review

Identification and Isolation of an Azoreductase from Enterococcus faecium

by
Susan R. Macwana
*,
Sumit Punj
,
John Cooper
,
Evan Schwenk
and
Gilbert H. John
Department of Microbiology and Molecular Genetics, Oklahoma State University, 418 LSE, Oklahoma State University Stillwater, OK 74075, USA
*
Author to whom correspondence should be addressed.
Curr. Issues Mol. Biol. 2010, 12(1), 43-48; https://doi.org/10.21775/cimb.012.043
Submission received: 2 May 2009 / Revised: 5 May 2009 / Accepted: 10 July 2009 / Published: 10 September 2009

Abstract

Azo dyes are commonly used in many commercial industries. Some of the azo dyes can produce carcinogenic compounds after being metabolized by azoreductase. Several human intestinal microbiota possess azoreductase activity which plays an important role in the toxicity and mutagenicity of these azo dye compounds. The acpD gene product (AzoEf1) responsible for the azoreductase activity of Enterococcus faecium, an intestinal bacterium, was heterologously expressed, purified and characterized. The protein sequence shares 67% identity with the azoreductase from Enterococcus faecalis, AzoA. Although AzoEf1 possesses many commonalities with AzoA, there are differences in coenzyme preference, residues associated with FMN binding, substrate specificity, and specific activity. AzoEf1 utilized both NADH and NADPH for the reduction of azo dyes, and it contains a leucyl residue at position 104 and threonyl residue at position 19 which differ from AzoA at the active site. Its specific activity was 5095 μM/min/mg and its catalytic efficiency for Methyl red reduction was lower than AzoA.
Keywords: acpD; AzoEf1; azoreductase; Enterococcus faecium; Enterococcus faecalis; AzoA; coenzyme preference; FMN binding; substrate specificity; specific activity acpD; AzoEf1; azoreductase; Enterococcus faecium; Enterococcus faecalis; AzoA; coenzyme preference; FMN binding; substrate specificity; specific activity

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MDPI and ACS Style

Macwana, S.R.; Punj, S.; Cooper, J.; Schwenk, E.; John, G.H. Identification and Isolation of an Azoreductase from Enterococcus faecium. Curr. Issues Mol. Biol. 2010, 12, 43-48. https://doi.org/10.21775/cimb.012.043

AMA Style

Macwana SR, Punj S, Cooper J, Schwenk E, John GH. Identification and Isolation of an Azoreductase from Enterococcus faecium. Current Issues in Molecular Biology. 2010; 12(1):43-48. https://doi.org/10.21775/cimb.012.043

Chicago/Turabian Style

Macwana, Susan R., Sumit Punj, John Cooper, Evan Schwenk, and Gilbert H. John. 2010. "Identification and Isolation of an Azoreductase from Enterococcus faecium" Current Issues in Molecular Biology 12, no. 1: 43-48. https://doi.org/10.21775/cimb.012.043

APA Style

Macwana, S. R., Punj, S., Cooper, J., Schwenk, E., & John, G. H. (2010). Identification and Isolation of an Azoreductase from Enterococcus faecium. Current Issues in Molecular Biology, 12(1), 43-48. https://doi.org/10.21775/cimb.012.043

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