The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Azoreductase: a key player of xenobiotic metabolism
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Azoreductases reduce azo dyes to their respective aromatic amines, resulting in reduced toxicity compared to the original molecules.
“In contrast, azoreductases are a class of enzymes capable of reducing azo dyes to their respective aromatic amines, resulting in reduced toxicity compared to the original molecules [196,197].”
From Recent Advances in the Remediation of Textile-Dye-Containing Wastewater: Prioritizing Human Health and Sustainable Wastewater Treatment (2024) · cites this paper as [197]
The Introduction says azoreductases cleave azo bonds and metabolize azo compounds to aromatic amines. It describes degradation as a detoxification pathway but cautions that the resulting metabolites can sometimes be more carcinogenic, so it does not support the unqualified claim that the amines are less toxic than the original dyes. (LLM, conf=0.90)
Experimental — accuracy not yet measuredAzoreductases are typically pH-stable within the range of 5-9, and their activity is at its peak under physiological conditions.
“Azoreductases are typically pH-stable within the range of 5-9, and their activity is at its peak under physiological conditions [197]”
From Recent Advances in the Remediation of Textile-Dye-Containing Wastewater: Prioritizing Human Health and Sustainable Wastewater Treatment (2024) · cites this paper as [197]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Chemical transformation of xenobiotics by the human gut microbiota
Koppel, N., Maini Rekdal, V., & Balskus, E. P. (2017) · Science · doi:10.1126/science.aag2770 · Cited by 1,080
Enzyme Sensitive Synthetic Polymer Micelles Based on the Azobenzene Motif
Rao, J., & Khan, A. (2013) · Journal of the American Chemical Society · doi:10.1021/ja407514z · Cited by 207
Chen, H., Wang, R.-F., & Cerniglia, C. E. (2004) · Protein Expression and Purification · doi:10.1016/j.pep.2003.12.016 · Cited by 180
Identification, Isolation and characterization of a novel azoreductase from Clostridium perfringens
Morrison, J. M., Wright, C. M., & John, G. H. (2012) · Anaerobe · doi:10.1016/j.anaerobe.2011.12.006 · Cited by 72
Flagged first, then by citations
Research works printed but not linked: 63
- Abraham KJ, John GH (2007) Development of a classification scheme using a secondary and tertiary amino acid analysis of azoreductase gene. J Med Biol Sci 1:1–5
- Bafana A, Chakrabarti T (2008) Lateral gene transfer in phylogeny of azoreductase enzyme. Comput Biol Chem 32:191–197 · DOI
- Bin Y, Jiti Z, Jing W, Cuihong D, Hongman H, Zhiyong S, Yongming B (2004) Expression and characteristics of the gene encoding azoreductase from Rhodobacter sphaeroides AS1.1737. FEMS Microbiol Lett 236:129–136 · DOI
- Blumel S, Stolz A (2003) Cloning and characterization of the gene coding for the aerobic azoreductase from Pigmentiphaga kullae K24. Appl Microbiol Biotechnol 62:186–190 · DOI
- Blumel S, Knackmuss HJ, Stolz A (2002) Molecular cloning and characterization of the gene coding for the aerobic azoreductase from Xenophilus azovorans KF46F. Appl Environ Microbiol 68:3948–3955 · DOI
- Bryant C, DeLuca M (1991) Purification and characterization of an oxygen-insensitive NAD(P)H nitroreductase from Enterobacter cloacae. J Biol Chem 266:4119–41125 · DOI
- Bürger S, Stolz A (2010) Characterization of the flavin-free oxygen-tolerant azoreductase from Xenophilus azovorans KF46F in comparison to flavin-containing azoreductases. Appl Microbiol Biotechnol 87:2067–2076 · DOI
- Chen H, Hopper SL, Cerniglia CE (2005) Biochemical and molecular characterization of an azoreductase from Staphylococcus aureus, a tetrameric NADPH-dependent flavoprotein. Microbiology 151:1433–1441 · DOI
- Chen H, Feng J, Kweon O, Xu H, Cerniglia CE (2010) Identification and molecular characterization of a novel flavin-free NADPH preferred azoreductase encoded by azo B in Pigmentiphaga kullae K24. BMC Biochem 11:13 · DOI
- Chung KT, Cerniglia CE (1992) Mutagenicity of azo dyes: structure-activity relationships. Mutat Res 277:201–220 · DOI
- Eslami M, Amoozegar MA, Asad S (2016) Isolation, cloning and characterization of an azoreductase from the halophilic bacterium Halomonas elongate. Int J Biol Macromol 85:111–116 · DOI
- Garau J (2008) Other antimicrobials of interest in the era of extended-spectrum beta-lactamases: fosfomycin, nitrofurantoin and tigecycline. Clin Microbiol Infect 1:198–202 · DOI
- Gonçalves AM, Mendes S, de Sanctis D, Martins LO, Bento I (2013) The crystal structure of Pseudomonas putida azoreductase-the active site revisited. FEBS J 280:6643–6657 · DOI
- Hervas M, Lopez-Maury L, Leon P, Sanchez-Riego AM, Florencio FJ, Navarro JA (2012) ArsH from the cyanobacterium Synechocystis sp. PCC 6803 is an efficient NADPH-dependent quinone reducatse. Biochemistry 51:1178–1187 · DOI
- Hu TL (2001) Kinetics of azoreductase and assessment of toxicity of metabolic products from azo dyes by Pseudomonas luteola. Water Sci Technol 43:261–269
- Idaka E, Horitsu H, Ogawa T (1987) Some properties of azoreductase produced by Pseudomonas cepacia. Bull Environ Contam Toxicol 39:982–989 · DOI
- Ito K, Nakanishi M, Lee WC, Zhi Y, Sasaki H, Zenno S, Saigo K, Kitade Y, Tanokura M (2008) Expansion of substrate specificity and catalytic mechanism of azoreductase by X-ray crystallography and site-directed mutagenesis. J Biol Chem 283:13889–13896 · DOI
- Kudlich M, Keck A, Klein J, Stolz A (1997) Localization of the enzyme system involved in the anaerobic reduction of azo dyes by Sphingomonas sp. strain BN6 and effect of artificial redox mediators on the rate of azo dye reduction. Appl Environ Microbiol 63:3691–3694 · DOI
- Lang W, Sirisansaneeyakul S, Ngiwsara L, Mendes S, Martins LO, Okuyama M, Kimura A (2013) Characterization of a new oxygen-insensitive azoreductase from Brevibacillus laterosporus TISTR1911: toward dye decolorization using a packed-bed metal affinity reactor. Bioresour Technol 150:298–306 · DOI
- Lautenschlager C, Schmidt C, Fischer D, Stallmach A (2014) Drug delivery strategies in the therapy of inflammatory bowel disease. Adv Drug Deliv Rev 71:58–76 · DOI
- Liu ZJ, Chen H, Shaw N, Hopper SL, Chen L, Chen S, Cerniglia CE, Wang BC (2007) Crystal structure of an aerobic FMN-dependent azoreductase (AzoA) from Enterococcus faecalis. Arch Biochem Biophys 463:68–77 · DOI
- Liu G, Zhou J, Jin R, Zhou M, Wang J, Lu H, Qu Y (2008) Enhancing survival of Escherichia coli by expression of azoreductase AZR possessing quinone reductase activity. Appl Microbiol Biotechnol 80:409–416 · DOI
- Liu G, Zhou J, Fu QS, Wang J (2009) The Escherichia coli azoreductase AzoR is involved in resistance to thiol-specific stress caused by electrophilic quinones. J Bacteriol 191:6394–6400 · DOI
- Liu F, Xu M, Chen X, Yang Y, Wang H, Sun G (2015) Novel strategy for tracking the microbial degradation of azo dyes with different polarities in living cells. Environ Sci Technol 49:11356–11362 · DOI
- Matsumoto K, Mukai Y, Ogata D, Shozui F, Nduko JM, Taguchi S, Ooi T (2010) Characterization of thermostable FMN-dependent NADH azoreductase from the moderate thermophile Geobacillus stearothermophilus. Appl Microbiol Biotechnol 86:1431–1438 · DOI
- McMullan G, Meehan C, Conneely C, Kirby N, Robinson T, Nigam P, Banat IM, Marchant R, Smyth WF (2001) Microbial decolorization and degradation of textile dyes. Appl Microbiol Biotechnol 56:81–87 · DOI
- Mendes S, Farinha A, Ramos CG, Leitao JH, Viegas CA, Martins LO (2011) Synergistic action of azoreductase and laccase leads to maximal decolourization and detoxification of model dye-containing wastewaters. Bioresour Technol 102:9852–9859 · DOI
- Misal SA, Lingojwar DP, Shinde RM, Gawai KR (2011) Purification and characterization of azoreductase from alkaliphilic strain Bacillus badius. Process Biochem 46:1264–1269 · DOI
- Misal SA, Lingojwar DP, Gawai KR (2013) Properties of NAD(P)H azoreductase from alkaliphilic red bacteria Aquiflexum sp. DL6. Protein J 32:601–608 · DOI
- Misal SA, Lingojwar DP, Lokhande MN, Lokhande PD, Gawai KR (2014) Enzymatic transformation of nitro-aromatic compounds by a flavin-free NADH azoreductase from Lysinibacillus sphaericus. Biotechnol Lett 36:127–131 · DOI
- Misal SA, Humne VT, Lokhande PD, Gawai KR (2015) Biotransformation of nitro aromatic compounds by flavin-free NADH-azoreductase. J Bioremed Biodeg 6:2–6 · DOI
- Morrison JM, John GH (2015) Non-classical azoreductase secretion in Clostridium perfringens in response to sulfonated azo dye exposure. Anaerobe 34:34–43 · DOI
- Nachiyar CV, Rajakumar GS (2005) Purification and characterization of an oxygen insensitive azoreductase from Pseudomonas aeruginosa. Enz Microbiol Technol 36:503–509 · DOI
- Nakanishi M, Yatome C, Ishida N, Kitade Y (2001) Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase. J Biol Chem 276:46394–46399 · DOI
- Nissen MS, Youn B, Knowles BD, Ballinger JW, Jun SY, Belchik SM, Xun L, Kang CH (2008) Crystal structures of NADH:FMN oxidoreductase (EmoB) at different stages of catalysis. J Biol Chem 283:28710–28720 · DOI
- Ooi T, Shibata T, Sato R, Ohno H, Kinoshita S, Thuoc TL, Taguchi S (2007) An azoreductase, aerobic NADH-dependent flavoprotein discovered from Bacillus sp.: functional expression and enzymatic characterization. Appl Microbiol Biotechnol 75:377–386 · DOI
- Ooi T, Shibata T, Matsumoto K, Kinoshita S, Taguchi S (2009) Comparative enzymatic analysis of azoreductases from Bacillus sp. B29. Biosci Biotechnol Biochem 73:1209–1211 · DOI
- Oturkar CC, Othman MA, Kulkarni M, Madamwar D, Gawai KR (2013) Synergistic action of flavin containing NADH dependent azoreductase and cytochrome P450 monooxygenase in azoaromatic mineralization. RSC adv 3:3062–3070 · DOI
- Punj S, John GH (2009) Purification and Identification of an FMN-dependent NAD(P)H azoreductase from Enterococcus faecalis. Curr Issues Mol Biol 11:59–66
- Qi J, Schlömann M, Tischler D (2016) Biochemical characterization of an azoreductase from Rhodococcus opacus 1CP possessing methyl red degradation ability. J Mol Catal B-Enzym 130:9–17 · DOI
- Qi J, Anke MK, Szymańska K, Tischler D (2017a) Immobilization of Rhodococcus opacus 1CP azoreductase to obtain azo dye degrading biocatalysts operative at acidic pH. Int Biodeterior Biodegrad 118:89–94 · DOI
- Qi J, Paul CE, Hollmann F, Tischler D (2017b) Changing the electron donor improves azoreductase dye degrading activity at neutral pH. Enz Microbiol Technol 100:17–19 · DOI
- Rafii F, Cerniglia CE (1995) Reduction of azo dyes and nitro aromatic compounds by bacterial enzymes from the human intestinal tract. Environ Health Persp 103:17–19 · DOI
- Rafii F, Coleman T (1999) Cloning and expression in Escherichia coli of an azoreductase gene from Clostridium perfringens and comparison with azoreductase genes from other bacteria. J Basic Microbiol 39:29–35 · DOI
- Rafii F, Franklin W, Cerniglia CE (1990) Azoreductase activity of anaerobic bacteria isolated from human intestinal micro flora. Appl Environ Microbiol 56:2146–2151 · DOI
- Robinson T, McMullan G, Marchant R, Nigam P (2001) Remediation of dyes in textile effluent: a critical review on current treatment technologies with a proposed alternative. Bioresour Technol 77:247–255 · DOI · Paper page
- Russ R, Rau J, Stolz A (2000) The function of cytoplasmic flavin reductases in the reduction of azo dyes by bacteria. Appl Environ Microbiol 66:1429–1434 · DOI
- Ryan A (2017) Azoreductases in drug metabolism. Br J Pharmacol 174(14):2161–2173 · DOI
- Ryan A, Laurieri N, Westwood I, Wang CJ, Lowe E, Sim E (2010a) A novel mechanism for azoreduction. J Mol Biol 400:24–37 · DOI
- Ryan A, Wang CJ, Laurieri N, Westwood I, Sim E (2010b) Reaction mechanism of azoreductases suggests convergent evolution with quinone oxidoreductases. Protein Cell 1:780–790 · DOI
- Ryan A, Kaplan E, Laurieri N, Lowe E, Sim E (2011) Activation of nitrofurazone by azoreductases: multiple activities in one enzyme. Sci Rep 1:63. https://doi.org/10.1038/srep00063 · DOI
- Ryan A, Kaplan E, Nebel JC, Polycarpou E, Crescente V et al (2014) Identification of NAD(P)H quinone oxidoreductase activity in azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone oxidoreductases belong to the same FMN-dependent superfamily of enzymes. PLoS ONE 9:e98551 · DOI
- Shin N, Hanaoka K, Piao W, Miyakawa T, Fujisawa T, Takeuchi S, Takahashi S, Komatsu T, Ueno T, Terai T, Tahara T, Tanokura M, Nagano T, Urano Y (2017) Development of an azoreductase-based reporter system with synthetic fluorogenic substrates. ACS Chem Biol 12:558–563 · DOI
- Stolz A (2001) Basic and applied aspects in the microbial degradation of azo dyes. Appl Microbiol Biotechnol 56:69–80 · DOI · Paper page
- Suzuki Y, Yoda T, Ruhul A, Sugiura W (2001) Molecular cloning and characterization of the gene coding for azoreductase from Bacillus sp. OY1-2 isolated from soil. J Biol Chem 276:9059–9065 · DOI
- Vijayalakshmidevi SR, Muthukumar K (2015) Improved biodegradation of textile dye effluent by coculture. Ecotoxicol Environ Saf 114:23–30 · DOI
- Wang CJ, Hagemeier C, Rahman N, Lowe E, Noble M, Coughtrie M, Sim E, Westwood I (2007) Molecular cloning, characterisation and ligand-bound structure of an azoreductase from Pseudomonas aeruginosa. J Mol Biol 373:1213–1228 · DOI
- Wang CJ, Laurieri N, Abuhammad A, LoourE Westwood I, Ryan A, Sim E (2010) Role of tyrosine 131 in the active site of paAzoR1, an azoreductase with specificity for the inflammatory bowel disease prodrug balsalazide. Acta Crystallogr Sect F Struct Biol Cryst Commun 66:2–7 · DOI
- Yang Y, Lu L, Gao F, Zhao Y (2013) Characterization of an efficient catalytic and organic solvent-tolerant azoreductase toward methyl red from Shewanella oneidensis MR-1. Environ Sci Pollut Res Int 20:3232–3239 · DOI
- Yu J, Ogata D, Gai Z, Taguchi S, Tanaka I, Ooi T, Yao M (2014) Structures of AzrA and of AzrC complexed with substrate or inhibitor: insight into substrate specificity and catalytic mechanism. Acta Crystallogr D Biol Crystallogr 70:553–564 · DOI
- Zhang X, Ng IS, Chang JS (2016) Cloning and characterization of a robust recombinant azoreductase from Shewanella xiamenensis BC01. J Taiwan Inst Chem E 61:97–105 · DOI
- Zimmermann T, Kulla HG, Leisinger T (1982) Properties of purified Orange II azoreductase, the enzyme initiating azo dye degradation by Pseudomonas KF46. Eur J Biochem 129:197–203 · DOI
- Zimmermann T, Gasser F, Kulla HG, Leisinger T (1984) Comparison of two azoreductases acquired during adaptation to growth on azo dyes. Arch Microbiol 138:37–43 · DOI
Cited by
Sorted by citations
Periyasamy, A. P. (2024) · Sustainability · doi:10.3390/su16020495 · Cited by 652
Emadi, Z., Sadeghi, M., & Forouzandeh, S. (2025) · Avicenna Journal of Environmental Health Engineering · doi:10.34172/ajehe.5491 · Cited by 4
Metadata
- Authors
- Misal, S. A., & Gawai, K. R.
- Venue
- Bioresources and Bioprocessing
- Published
- 2018-04-26
- Volume
- 5
- Issue
- 1
- ISSN
- 2197-4365
- Cited by
- 184
- References
- 4
- Language
- en
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review