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DioxygenasesOxygenasesCatechol 2,3-DioxygenaseCatecholsProtocatechuate-3,4-DioxygenaseNAD(P)H Dehydrogenase (Quinone)Quinone ReductasesCatechol 1,2-DioxygenaseRhodococcusPyruvate SynthaseOxidoreductasesNonheme Iron ProteinsKetoglutaric AcidsSphingomonasBiodegradation, EnvironmentalRalstoniaMixed Function OxygenasesMolecular Sequence DataNADH, NADPH OxidoreductasesSubstrate Specificity2-Methyl-4-chlorophenoxyacetic AcidElectron Transport Complex IHydrocarbons, CyclicPseudomonasAmino Acid SequenceXanthine DehydrogenaseOxidation-ReductionPseudomonas putidaDelftia acidovoransBurkholderiaSequence Homology, Amino AcidFerrous CompoundsHomogentisic AcidProtochlorophyllideKineticsArthrobacterPetroselinumElectron Spin Resonance SpectroscopyEscherichia coliIron-Sulfur ProteinsIronProtein Disulfide Reductase (Glutathione)FerredoxinsOxidoreductases Acting on CH-CH Group DonorsProcollagen-Proline DioxygenaseCloning, MolecularCatalysisChlorobenzenesNADPH-Ferrihemoprotein ReductaseCysteine DioxygenaseDicumarolHydroquinonesFlavin MononucleotideBiphenyl CompoundsGenes, BacterialHydroxylationBacterial ProteinsFMN ReductaseHydroxybenzoatesFerredoxin-NADP ReductaseOxygenNADFlavin-Adenine DinucleotideElectron TransportKetone OxidoreductasesSequence AlignmentGentisatesModels, MolecularPolychlorinated BiphenylsNADPTryptophan OxygenaseBase SequenceElectron Transport Complex IIIGallic AcidNADH DehydrogenaseElectron Transport Complex IIBinding SitesIndigo CarmineAlcohol OxidoreductasesSpectrophotometryRecombinant ProteinsChlorobenzoatesAcinetobacterCatalytic DomainGram-Negative Aerobic BacteriaUbiquinoneNitrosomonasBacteria, AerobicParabensXanthine OxidaseModels, ChemicalNorisoprenoidsMultigene FamilyCrystallography, X-RayHerbicidesFlavoproteinsPhylogenyToluene2,2'-Dipyridyl4-Hydroxyphenylpyruvate Dioxygenase

PutativeAlpha-ketoglutarate dioxygenaseReductaseEscherichiaEnzymesOxygenaseActing on pairedProteinsSystematic1.13.11.11ClassificationOxidaseDioxygenCatecholEnzymologyInterproscanSubunitSuperfamilyOxidationSubstratesIdentificationIronIncludeActivationOxygenasesEnzymeFerredoxinIndoleamineExtradiolPseudomonasGibberellinHemeDomainSingle

Putative2

• Negative regulator of flavonoid biosynthesis, mutants accumulate flavonoid pigments in their seed coat, putative oxidoreductase. (or.jp)
• SCO7572 putative oxidoreductase 8394796:8397792 forward MW:106693 0054. (kitasato-u.ac.jp)

Alpha-ketoglutarate dioxygenase1

• Cloning and characterization of a sulfonate/alpha-ketoglutarate dioxygenase from Saccharomyces cerevisiae. (ymdb.ca)

Reductase2

• Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. (nih.gov)
• In dioxygenase FAD/NAD(P) binding domain, the reductase transfers 2 electrons from NAD(P)H to the oxygenase which insert into an aromatic substrate, an initial step in microbial aerobic degradation of aromatic rings. (nih.gov)

Escherichia3

• The concepts of his Pseudomonas putida study are interwoven with issues in Escherichia coli, Electron donor, Dioxygenase, Dehydrogenase and Naphthalene. (research.com)
• His Pseudomonas putida research is multidisciplinary, incorporating elements of Nuclear chemistry, Escherichia coli, Toluene, Chromatography and Toluene dioxygenase. (research.com)
• His Escherichia coli research integrates issues from Regioselectivity, Microorganism, Pseudomonas putida, Metabolite and Toluene dioxygenase. (research.com)

Enzymes2

• Dioxygenases are oxidoreductase enzymes. (wikipedia.org)
• The catechol dioxygenases, some of the most well-studied dioxygenase enzymes, use dioxygen to cleave a carbon-carbon bond of an aromatic catechol ring system. (wikipedia.org)

Oxygenase1

• Other names in common use include thymine 7-hydroxylase, 5-hydroxy-methyluracil dioxygenase, and 5-hydroxymethyluracil oxygenase. (wikipedia.org)

Acting on paired1

• This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. (wikipedia.org)

Proteins1

• As a Class I bacterial dioxygenases, benzoate dioxygenase like proteins combine an [2Fe-2S] cluster containing N-terminal ferredoxin at the end fused to an FAD/NADP(P) domain. (nih.gov)

Systematic1

• The systematic name of this enzyme class is thymine,2-oxoglutarate:oxygen oxidoreductase (7-hydroxylating). (wikipedia.org)

1.13.11.111

• This enzyme has broader substrate specificity than EC 1.13.11.11 , tryptophan 2,3-dioxygenase [1]. (genome.jp)

Classification1

• Enzyme classification.EC_1 oxidoreductases.EC_1.14. (ntu.edu.sg)

Oxidase1

• Involved in the abscisic-acid biosynthesis pathway in plants, along with EC 1.2.3.14 (abscisic-aldehyde oxidase), EC 1.13.11.51 (9- cis -epoxycarotenoid dioxygenase) and EC 1.14.13.93 [(+)-abscisic acid 8′-hydroxylase]. (enzyme-database.org)

Dioxygen5

• The dioxygenases (EC 1.13.11) catalyze the oxidation of a substrate without the reduction of one oxygen atom from dioxygen into a water molecule. (wikipedia.org)
• The majority of dioxygenases fully incorporate dioxygen into a single substrate, and a variety of cofactor schemes are utilized to achieve this. (wikipedia.org)
• The mononuclear iron dioxygenases, or non-heme iron-dependent dioxygenases as they are also termed, all utilize a single catalytic iron to incorporate either one or both atoms of dioxygen into a substrate. (wikipedia.org)
• Despite this common oxygenation event, the mononuclear iron dioxygenases are diverse in how dioxygen activation is used to promote certain chemical reactions. (wikipedia.org)
• Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron. (research.com)

Catechol2

• Two important groups of mononuclear, non-heme iron dioxygenases are catechol dioxygenases and 2-oxoglutarate (2OG)-dependent dioxygenases. (wikipedia.org)
• Catechol dioxygenases are further classified as being "extradiol" or "intradiol," and this distinction is based on mechanistic differences in the reactions (figures 1 & 2). (wikipedia.org)

Enzymology1

• In enzymology, a thymine dioxygenase (EC 1.14.11.6) is an enzyme that catalyzes the chemical reaction thymine + 2-oxoglutarate + O2 ⇌ {\displaystyle \rightleftharpoons } 5-hydroxymethyluracil + succinate + CO2 The 3 substrates of this enzyme are thymine, 2-oxoglutarate, and O2, whereas its 3 products are 5-hydroxymethyluracil, succinate, and CO2. (wikipedia.org)

Interproscan1

• Molydopterin dinucleotide binding domain, Molybdopterin oxidoreductase Fe4S4 domain [Interproscan]. (ntu.edu.sg)

Subunit1

• MSMEG_3676 MSMEG_3676 Phenoxybenzoate dioxygenase beta subunit (EC 1. (systemsbiology.net)

Superfamily1

• Most mononuclear iron dioxygenases are members of the cupin superfamily in which the overall domain structure is described as a six-stranded β-barrel fold (or jelly roll motif). (wikipedia.org)

Oxidation1

• For instance, carbon-carbon bond cleavage, fatty acid hydroperoxidation, carbon-sulfur bond cleavage, and thiol oxidation are all reactions catalyzed by mononuclear iron dioxygenases. (wikipedia.org)

Substrates1

• Flavin oxidoreductases use flavins as substrates, unlike flavoenzymes which have a flavin prosthetic group. (nih.gov)

Identification1

• Identification of two alpha-ketoglutarate-dependent dioxygenases in extracts of Rhodotorula glutinis catalyzing deoxyuridine hydroxylation. (genome.jp)

Iron2

• Iron-containing dioxygenases can be subdivided into three classes on the basis of how iron is incorporated into the active site: those employing a mononuclear iron center, those containing a Rieske [2Fe-2S] cluster, and those utilizing a heme prosthetic group. (wikipedia.org)
• In the 2OG-dependent dioxygenases, ferrous iron (Fe(II)) is also coordinated by a (His)2(Glu/Asp)1 "facial triad" motif. (wikipedia.org)

Include1

• His primary areas of investigation include Organic chemistry, Toluene dioxygenase, Pseudomonas putida, Biochemistry and NAD+ kinase. (research.com)

Activation1

• The limiting step for its initiation is activation of two oxidoreductases-indolamine-2,3-dioxygenase (IDO) and tryptophan-2,3-dioxygenase (TDO). (encyclopedia.pub)

Oxygenases1

• This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O 2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). (alchetron.com)

Enzyme9

• In enzymology, a thymine dioxygenase (EC 1.14.11.6) is an enzyme that catalyzes the chemical reaction thymine + 2-oxoglutarate + O2 ⇌ {\displaystyle \rightleftharpoons } 5-hydroxymethyluracil + succinate + CO2 The 3 substrates of this enzyme are thymine, 2-oxoglutarate, and O2, whereas its 3 products are 5-hydroxymethyluracil, succinate, and CO2. (wikipedia.org)
• This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. (wikipedia.org)
• The systematic name of this enzyme class is thymine,2-oxoglutarate:oxygen oxidoreductase (7-hydroxylating). (wikipedia.org)
• 4Fe-4S dicluster domain, Domain of unknown function, Thiamine pyrophosphate enzyme, Pyruvate ferredoxin/flavodoxin oxidoreductase, Pyruvate flavodoxin/ferredoxin oxidoreductase, Pyruvate:ferredoxin oxidoreductase core domain II [Interproscan]. (ntu.edu.sg)
• The systematic name of this enzyme class is 1-hydroxy-2-naphthoate:oxygen 1,2-oxidoreductase (decyclizing) . (alchetron.com)
• Other names in common use include 1-hydroxy-2-naphthoate dioxygenase , 1-hydroxy-2-naphthoate-degrading enzyme , and 1-hydroxy-2-naphthoic acid dioxygenase . (alchetron.com)
• PTGS1 (COX1, Cyclooxygenase 1) is the key enzyme in prostaglandin biosynthesis, and acts both as a dioxygenase and as a peroxidase. (thermofisher.com)
• Enzyme classification.EC_1 oxidoreductases.EC_1.14. (ntu.edu.sg)
• In this study, we kept 14CoS/14CoS mice alive for 60 d with oral 2-(2-nitro-4-trifluoromethyl-benzyol)-1,3-cyclohexanedione (NTBC), an inhibitor of p-hydroxyphenylpyruvate dioxygenase, second enzyme in the tyrosine catabolic pathway. (nih.gov)

Ferredoxin1

• 19. Insights into Flavin-based Electron Bifurcation via the NADH-dependent Reduced Ferredoxin:NADP Oxidoreductase Structure. (nih.gov)

Indoleamine2

• A dioxygenase with specificity for the oxidation of the indoleamine ring of TRYPTOPHAN . (nih.gov)
• Indoleamine 2,3-dioxygenase (IDO), a single chain oxidoreductase that serves as a catalyst for the degradation of tryptophan into kynurenine, has emerged as a critical player in T-cell suppression and the induction of immune tolerance to tumors. (augusta.edu)

Extradiol1

• Catechol dioxygenases are further classified as being "extradiol" or "intradiol," and this distinction is based on mechanistic differences in the reactions (figures 1 & 2). (wikipedia.org)

Pseudomonas1

• 10. Structural Analysis Provides Mechanistic Insight into Nicotine Oxidoreductase from Pseudomonas putida. (nih.gov)

Gibberellin3

• Glycine max gibberellin 2-beta-dioxygenase 6 (GA2OX6), mRNA. (go.jp)
• Vigna angularis gibberellin 2-beta-dioxygenase 1-like (LOC108332455), mRNA. (go.jp)
• Gibberellin 3-beta-dioxygenase. (uma.es)

Heme3

• Iron-containing dioxygenases can be subdivided into three classes on the basis of how iron is incorporated into the active site: those employing a mononuclear iron center, those containing a Rieske [2Fe-2S] cluster, and those utilizing a heme prosthetic group. (wikipedia.org)
• The mononuclear iron dioxygenases, or non-heme iron-dependent dioxygenases as they are also termed, all utilize a single catalytic iron to incorporate either one or both atoms of dioxygen into a substrate. (wikipedia.org)
• Two important groups of mononuclear, non-heme iron dioxygenases are catechol dioxygenases and 2-oxoglutarate (2OG)-dependent dioxygenases. (wikipedia.org)

Domain2

• Most mononuclear iron dioxygenases are members of the cupin superfamily in which the overall domain structure is described as a six-stranded β-barrel fold (or jelly roll motif). (wikipedia.org)
• 11. Structure of the membrane proximal oxidoreductase domain of human Steap3, the dominant ferrireductase of the erythroid transferrin cycle. (nih.gov)

Single1

• The majority of dioxygenases fully incorporate dioxygen into a single substrate, and a variety of cofactor schemes are utilized to achieve this. (wikipedia.org)