{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T09:49:36Z","timestamp":1791107376960,"version":"4.1.0"},"reference-count":52,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2006,2,15]]},"abstract":"<jats:p>Shewanella oneidensis contains four genes that encode proteins that have high sequence identity with yeast OYE (Old Yellow Enzyme, an NADPH oxidoreductase), the well-studied archetype of the OYE protein family. The present paper describes the first comparative study of OYEs that are present in a single bacterial species, performed to gain insight into their biochemical properties and physiological importance. The four proteins [named SYE1\u2013SYE4 (Shewanella Yellow Enzyme 1\u20134)] were expressed as glutathione S-transferase fusion proteins in Escherichia coli. The yield of SYE2, however, was too low for further characterization, even after expression attempts in S. oneidensis. The SYE1, SYE3 and SYE4 proteins were found to have characteristics similar to those of other OYE family members. They were identified as flavoproteins that catalyse the reduction of different \u03b1,\u03b2-unsaturated carbonyl compounds and form charge transfer complexes with a range of phenolic compounds. Whereas the properties of SYE1 and SYE3 were very similar, those of SYE4 were clearly different in terms of ligand binding, catalytic efficiency and substrate specificity. Also, the activity of SYE4 was found to be NADPH-dependent, whereas SYE1 and SYE3 had a preference for NADH. It has been suggested that yeast OYE protects the actin cytoskeleton from oxidative stress. There are indications that bacterial OYEs are also involved in the oxidative stress response, but their exact role is unclear. Induction studies in S. oneidensis revealed that yeast and bacterial OYEs may share a common physiological role, i.e. the protection of cellular components against oxidative damage. As only SYE4 was induced under oxidative stress conditions, however, a functional divergence between bacterial OYEs is likely to exist.<\/jats:p>","DOI":"10.1042\/bj20050979","type":"journal-article","created":{"date-parts":[[2006,3,2]],"date-time":"2006-03-02T09:17:57Z","timestamp":1141291077000},"page":"335-344","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":57,"title":["Comparative characterization and expression analysis of the four Old Yellow Enzyme homologues from <i>Shewanella oneidensis<\/i> indicate differences in physiological function"],"prefix":"10.1042","volume":"394","author":[{"given":"Ann","family":"Brig\u00e9","sequence":"first","affiliation":[{"name":"Laboratory of Protein Biochemistry and Protein Engineering, Gent University, K.L. 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Z."},{"key":"2021112213273730200_B3","doi-asserted-by":"crossref","first-page":"922","DOI":"10.1073\/pnas.91.3.922","article-title":"Candida albicans estrogen-binding protein gene encodes an oxidoreductase that is inhibited by estradiol","volume":"91","author":"Madani","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112213273730200_B4","doi-asserted-by":"crossref","first-page":"3002","DOI":"10.1128\/jb.175.10.3002-3012.1993","article-title":"Characterization of the baiH gene encoding a bile acid-inducible NADH:flavin oxidoreductase from Eubacterium sp. strain VPI 12708","volume":"175","author":"Franklund","year":"1993","journal-title":"J. Bacteriol."},{"key":"2021112213273730200_B5","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/0014-5793(92)81291-S","article-title":"Trimethylamine dehydrogenase of bacterium W3A1: molecular cloning, sequence determination and overexpression of the gene","volume":"308","author":"Boyd","year":"1992","journal-title":"FEBS Lett."},{"key":"2021112213273730200_B6","doi-asserted-by":"crossref","first-page":"6097","DOI":"10.1016\/S0021-9258(18)53224-5","article-title":"Old Yellow Enzyme: the discovery of multiple isozymes and a family of related proteins","volume":"268","author":"Stott","year":"1993","journal-title":"J. Biol. Chem."},{"key":"2021112213273730200_B7","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1002\/yea.320110509","article-title":"Nucleotide sequence and chromosomal localization of the gene encoding the Old Yellow Enzyme from Kluyveromyces lactis","volume":"11","author":"Miranda","year":"1995","journal-title":"Yeast"},{"key":"2021112213273730200_B8","doi-asserted-by":"crossref","first-page":"1983","DOI":"10.1074\/jbc.270.5.1983","article-title":"A new old yellow enzyme of Saccharomyces cerevisiae","volume":"270","author":"Niino","year":"1995","journal-title":"J. Biol. Chem."},{"key":"2021112213273730200_B9","doi-asserted-by":"crossref","first-page":"28066","DOI":"10.1074\/jbc.272.44.28066","article-title":"Molecular cloning and characterization of 12-oxophytodienoate reductase, an enzyme of the octadecanoid signaling pathway from Arabidopsis thaliana: structural and functional relationship to yeast Old Yellow Enzyme","volume":"272","author":"Schaller","year":"1997","journal-title":"J. Biol. Chem."},{"key":"2021112213273730200_B10","doi-asserted-by":"crossref","first-page":"1345","DOI":"10.1104\/pp.118.4.1345","article-title":"12-Oxophytodienoate-10,11-reductase: occurrence of two isoenzymes of different specificity against stereoisomers of 12-oxophytodienoic acid","volume":"118","author":"Schaller","year":"1998","journal-title":"Plant Physiol."},{"key":"2021112213273730200_B11","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1007\/s004250050545","article-title":"Structure and regulation of OPR1 and OPR2, two closely related genes encoding 12-oxophytodienoic acid-10,11-reductases from Arabidopsis thaliana","volume":"208","author":"Biesgen","year":"1999","journal-title":"Planta"},{"key":"2021112213273730200_B12","doi-asserted-by":"crossref","first-page":"35067","DOI":"10.1074\/jbc.274.49.35067","article-title":"A homolog of Old Yellow Enzyme in tomato: spectral properties and substrate specificity of the recombinant protein","volume":"274","author":"Strassner","year":"1999","journal-title":"J. Biol. Chem."},{"key":"2021112213273730200_B13","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1007\/s004250050706","article-title":"12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in jasmonate biosynthesis","volume":"210","author":"Schaller","year":"2000","journal-title":"Planta"},{"key":"2021112213273730200_B14","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1007\/s00294-002-0321-z","article-title":"Old yellow enzyme confers resistance of Hansenula polymorpha towards allyl alcohol","volume":"41","author":"Komduur","year":"2002","journal-title":"Curr. Genet."},{"key":"2021112213273730200_B15","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1084\/jem.20020885","article-title":"A key role for old yellow enzyme in the metabolism of drugs by Trypanosoma cruzi","volume":"196","author":"Kubata","year":"2002","journal-title":"J. Exp. Med."},{"key":"2021112213273730200_B16","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1007\/s00425-002-0909-z","article-title":"Cloning and characterization of a jasmonic acid-responsive gene encoding 12-oxophytodienoic acid reductase in suspension-cultured rice cells","volume":"216","author":"Sobajima","year":"2003","journal-title":"Planta"},{"key":"2021112213273730200_B17","doi-asserted-by":"crossref","first-page":"6623","DOI":"10.1128\/jb.178.22.6623-6627.1996","article-title":"Sequence and properties of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2","volume":"178","author":"French","year":"1996","journal-title":"J. Bacteriol."},{"key":"2021112213273730200_B18","doi-asserted-by":"crossref","first-page":"7796","DOI":"10.1128\/jb.179.24.7796-7802.1997","article-title":"Purification, properties, and sequence of glycerol trinitrate reductase from Agrobacterium radiobacter","volume":"179","author":"Snape","year":"1997","journal-title":"J. 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Bacteriol."},{"key":"2021112213273730200_B22","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1248\/bpb.20.110","article-title":"Molecular cloning of the nemA gene encoding N-ethylmaleimide reductase from Escherichia coli","volume":"20","author":"Miura","year":"1997","journal-title":"Biol. Pharm. Bull."},{"key":"2021112213273730200_B23","doi-asserted-by":"crossref","first-page":"19891","DOI":"10.1074\/jbc.M211778200","article-title":"Characterization of YqjM, an Old Yellow Enzyme homolog from Bacillus subtilis involved in the oxidative stress response","volume":"278","author":"Fitzpatrick","year":"2003","journal-title":"J. Biol. Chem."},{"key":"2021112213273730200_B24","doi-asserted-by":"crossref","first-page":"4246","DOI":"10.1021\/bi00013a014","article-title":"Old Yellow Enzyme: aromatization of cyclic enones and the mechanism of a novel dismutation reaction","volume":"34","author":"Vaz","year":"1995","journal-title":"Biochemistry"},{"key":"2021112213273730200_B25","doi-asserted-by":"crossref","first-page":"5327","DOI":"10.1016\/S0021-9258(17)33165-4","article-title":"Interaction of phenols with Old Yellow Enzyme: physical evidence for charge-transfer complexes","volume":"251","author":"Abramovitz","year":"1976","journal-title":"J. Biol. Chem."},{"key":"2021112213273730200_B26","doi-asserted-by":"crossref","first-page":"13639","DOI":"10.1016\/S0021-9258(17)38773-2","article-title":"Potentiometric studies of native and flavinsubstituted Old Yellow Enzyme","volume":"260","author":"Stewart","year":"1985","journal-title":"J. Biol. 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Chem."},{"key":"2021112213273730200_B28","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1016\/S0969-2126(94)00111-1","article-title":"Old yellow enzyme at 2 \u00c5 resolution: overall structure, ligand binding, and comparison with related flavoproteins","volume":"2","author":"Fox","year":"1994","journal-title":"Structure"},{"key":"2021112213273730200_B29","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1006\/jmbi.2001.4779","article-title":"Crystal structure of pentaerythritol tetranitrate reductase: \u2018flipped\u2019 binding geometries for steroid substrates in different redox states of the enzyme","volume":"310","author":"Barna","year":"2001","journal-title":"J. Mol. 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Chem."},{"key":"2021112213273730200_B33","doi-asserted-by":"crossref","first-page":"4522","DOI":"10.1091\/mbc.e04-06-0445","article-title":"Old yellow enzyme protects the actin cytoskeleton from oxidative stress","volume":"15","author":"Haarer","year":"2004","journal-title":"Mol. Biol. Cell"},{"key":"2021112213273730200_B34","doi-asserted-by":"crossref","first-page":"1118","DOI":"10.1038\/nbt749","article-title":"Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis","volume":"20","author":"Heidelberg","year":"2002","journal-title":"Nature Biotech."},{"key":"2021112213273730200_B35","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1111\/j.1574-6968.1999.tb13575.x","article-title":"BLAST 2 Sequences, a new tool for comparing protein and nucleotide sequences","volume":"174","author":"Tatusova","year":"1999","journal-title":"FEMS Microbiol. Lett."},{"key":"2021112213273730200_B36a","doi-asserted-by":"crossref","first-page":"4673","DOI":"10.1093\/nar\/22.22.4673","article-title":"CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice","volume":"22","author":"Higgins","year":"1994","journal-title":"Nucleic Acids Res."},{"key":"2021112213273730200_B36b","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature (London)"},{"key":"2021112213273730200_B37","doi-asserted-by":"crossref","first-page":"1802","DOI":"10.1128\/JB.186.6.1802-1810.2004","article-title":"Characterization of glycerol trinitrate reductase (NerA) and the catalytic role of active-site residues","volume":"186","author":"Marshall","year":"2004","journal-title":"J. Bacteriol."},{"key":"2021112213273730200_B38","doi-asserted-by":"crossref","first-page":"32753","DOI":"10.1074\/jbc.273.49.32753","article-title":"On the active site of Old Yellow Enzyme: role of histidine 191 and asparagine 194","volume":"273","author":"Brown","year":"1998","journal-title":"J. Biol. Chem."},{"key":"2021112213273730200_B39","doi-asserted-by":"crossref","first-page":"5321","DOI":"10.1016\/S0021-9258(17)33164-2","article-title":"Purification of intact old yellow enzyme using an affinity matrix for the sole chromatographic step","volume":"251","author":"Abramovitz","year":"1976","journal-title":"J. Biol. Chem."},{"key":"2021112213273730200_B40","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1021\/cr60165a003","article-title":"A reexamination of the Hammett equation","volume":"53","author":"Jaffe","year":"1953","journal-title":"Chem. Rev."},{"key":"2021112213273730200_B41","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1021\/cr00002a004","article-title":"A survey of Hammett substituent constants and resonance and field parameters","volume":"91","author":"Hansch","year":"1991","journal-title":"Chem. Rev."},{"key":"2021112213273730200_B42","doi-asserted-by":"crossref","first-page":"6912","DOI":"10.1128\/jb.179.22.6912-6920.1997","article-title":"Regioselectivity of nitroglycerin denitration by flavoprotein nitroester reductases purified from two Pseudomonas species","volume":"179","author":"Blehert","year":"1997","journal-title":"J. Bacteriol."},{"key":"2021112213273730200_B43","doi-asserted-by":"crossref","first-page":"7598","DOI":"10.1021\/bi980345i","article-title":"Reductive and oxidative half-reactions of morphinone reductase from Pseudomonas putida M10: a kinetic and thermodynamic analysis","volume":"37","author":"Craig","year":"1998","journal-title":"Biochemistry"},{"key":"2021112213273730200_B44","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1021\/bi00594a001","article-title":"Light-mediated reduction of flavoproteins with flavins as catalysts","volume":"17","author":"Massey","year":"1978","journal-title":"Biochemistry"},{"key":"2021112213273730200_B45","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1016\/j.pep.2004.04.012","article-title":"Structural and functional impairment of an Old Yellow Enzyme homologue upon affinity tag incorporation","volume":"36","author":"Fitzpatrick","year":"2004","journal-title":"Protein Expression Purif."},{"key":"2021112213273730200_B46","doi-asserted-by":"crossref","first-page":"2864","DOI":"10.1128\/AEM.64.8.2864-2868.1998","article-title":"Aerobic degradation of 2,4,6-trinitrotoluene by Enterobacter cloacae PB2 and by pentaerythritol tetranitrate reductase","volume":"64","author":"French","year":"1998","journal-title":"Appl. Environ. Microbiol."},{"key":"2021112213273730200_B47","doi-asserted-by":"crossref","first-page":"4742","DOI":"10.1128\/AEM.66.11.4742-4750.2000","article-title":"Transformation of 2,4,6-trinitrotoluene by purified xenobiotic reductase B from Pseudomonas fluorescens I-C","volume":"66","author":"Pak","year":"2000","journal-title":"Appl. Environ. Microbiol."},{"key":"2021112213273730200_B48","doi-asserted-by":"crossref","first-page":"3566","DOI":"10.1128\/AEM.70.6.3566-3574.2004","article-title":"Biotransformation of explosives by the old yellow enzyme family of flavoproteins","volume":"70","author":"Williams","year":"2004","journal-title":"Appl. Environ. Microbiol."},{"key":"2021112213273730200_B49","doi-asserted-by":"crossref","first-page":"7796","DOI":"10.1128\/JB.186.22.7796-7803.2004","article-title":"Global transcriptome analysis of the heat shock response of Shewanella oneidensis","volume":"186","author":"Gao","year":"2004","journal-title":"J. Bacteriol."},{"key":"2021112213273730200_B50","first-page":"72","article-title":"Formation of superoxide radical and hydrogen peroxide enhanced by trinitrotoluene in rat liver, brain, kidney, and testicle in vitro and monkey liver in vivo","volume":"2","author":"Kong","year":"1989","journal-title":"Biomed. Environ. Sci."},{"key":"2021112213273730200_B51","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1172\/JCI200419267","article-title":"Central role of mitochondrial aldehyde dehydrogenase and reactive oxygen species in nitroglycerin tolerance and cross-tolerance","volume":"113","author":"Sydow","year":"2004","journal-title":"J. Clin. 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