1oya Citations

Old yellow enzyme at 2 A resolution: overall structure, ligand binding, and comparison with related flavoproteins.

Structure 2 1089-105 (1994)
Related entries: 1oyc, 1oyb

Cited: 81 times
EuropePMC logo PMID: 7881908



Old yellow enzyme (OYE) was the first flavoenzyme purified, but its function is still unknown. Nevertheless, the NADPH oxidase activity, the flavin mononucleotide environment and the ligand-binding properties of OYE have been extensively studied by biochemical and spectroscopic approaches. Full interpretation of these data requires structural information.


The crystal structures of oxidized and reduced OYE at 2 A resolution reveal an alpha/beta-barrel topology clearly related to trimethylamine dehydrogenase. Complexes of OYE with p-hydroxybenzaldehyde, beta-estradiol, and an NADPH analog show all three binding at a common site, stacked on the flavin. The putative NADPH binding mode is novel as it involves primary recognition of the nicotinamide mononucleotide portion.


This work shows that the striking spectral changes seen upon phenol binding are due to close physical association of the flavin and phenolate. It also identifies the structural class of OYE and suggests that if NADPH is its true substrate, then OYE has adopted NADPH dependence during evolution.

Articles - 1oya mentioned but not cited (2)

  1. The combined structural and kinetic characterization of a bacterial nitronate monooxygenase from Pseudomonas aeruginosa PAO1 establishes NMO class I and II. Salvi F, Agniswamy J, Yuan H, Vercammen K, Pelicaen R, Cornelis P, Spain JC, Weber IT, Gadda G. J. Biol. Chem. 289 23764-23775 (2014)
  2. Structure of an Aspergillus fumigatus old yellow enzyme (EasA) involved in ergot alkaloid biosynthesis. Chilton AS, Ellis AL, Lamb AL. Acta Crystallogr F Struct Biol Commun 70 1328-1332 (2014)

Reviews citing this publication (5)

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  4. alpha-Amylase family: molecular biology and evolution. Janecek S. Prog. Biophys. Mol. Biol. 67 67-97 (1997)
  5. Structure of bacterial luciferase. Baldwin TO, Christopher JA, Raushel FM, Sinclair JF, Ziegler MM, Fisher AJ, Rayment I. Curr. Opin. Struct. Biol. 5 798-809 (1995)

Articles citing this publication (74)

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  26. Coenzyme binding in F420-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family. Aufhammer SW, Warkentin E, Berk H, Shima S, Thauer RK, Ermler U. Structure 12 361-370 (2004)
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  62. An engineered old yellow enzyme that enables efficient synthesis of (4R,6R)-Actinol in a one-pot reduction system. Horita S, Kataoka M, Kitamura N, Nakagawa T, Miyakawa T, Ohtsuka J, Nagata K, Shimizu S, Tanokura M. Chembiochem 16 440-445 (2015)
  63. Comprehensive genome-wide analysis reveals different classes of enigmatic old yellow enzyme in fungi. Nizam S, Verma S, Borah NN, Gazara RK, Verma PK. Sci Rep 4 4013 (2014)
  64. An enoate reductase Achr-OYE4 from Achromobacter sp. JA81: characterization and application in asymmetric bioreduction of C=C bonds. Wang HB, Pei XQ, Wu ZL. Appl. Microbiol. Biotechnol. 98 705-715 (2014)
  65. Further computational studies on the conformation of 1,5-dihydrolumiflavin. Rizzo CJ. Antioxid. Redox Signal. 3 737-746 (2001)
  66. Loop-Grafted Old Yellow Enzymes in the Bienzymatic Cascade Reduction of Allylic Alcohols. Reich S, Nestl BM, Hauer B. Chembiochem 17 561-565 (2016)
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  68. Pichia stipitis OYE 2.6 variants with improved catalytic efficiencies from site-saturation mutagenesis libraries. Patterson-Orazem A, Sullivan B, Stewart JD. Bioorg. Med. Chem. 22 5628-5632 (2014)
  69. Recombinant S. cerevisiae expressing Old Yellow Enzymes from non-conventional yeasts: an easy system for selective reduction of activated alkenes. Romano D, Contente ML, Molinari F, Eberini I, Ruvutuso E, Sensi C, Amaretti A, Rossi M, Raimondi S. Microb. Cell Fact. 13 60 (2014)
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  71. Structural insights into stereospecific reduction of α, β-unsaturated carbonyl substrates by old yellow enzyme from Gluconobacter oxydans. Yin B, Deng J, Lim L, Yuan YA, Wei D. Biosci. Biotechnol. Biochem. 79 410-421 (2015)
  72. α,β-Dicarbonyl reduction is mediated by the Saccharomyces Old Yellow Enzyme. van Bergen B, Cyr N, Strasser R, Blanchette M, Sheppard JD, Jardim A. FEMS Yeast Res. 16 (2016)
  73. Sequential Enzymatic Conversion of α-Angelica Lactone to γ-Valerolactone through Hydride-Independent C=C Bond Isomerization. Turrini NG, Eger E, Reiter TC, Faber K, Hall M. ChemSusChem 9 3393-3396 (2016)
  74. Mycobacterial F420H2-Dependent Reductases Promiscuously Reduce Diverse Compounds through a Common Mechanism. Greening C, Jirapanjawat T, Afroze S, Ney B, Scott C, Pandey G, Lee BM, Russell RJ, Jackson CJ, Oakeshott JG, Taylor MC, Warden AC. Front Microbiol 8 1000 (2017)