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Dioxygenases

Dioxygenases introduce both atoms of an oxygen molecule into substrates. In most instances the two oxygen atoms react with one substrate molecule (intramolecular dioxygenases)  [Pg.94]

Some dioxygenases, however, incorporate one atom each of the oxygen molecule into different molecules of the same substrate  [Pg.94]

In the last case one of the two substrates is invariably x-ketoglutaric acid. x-Ketoglutaric acid is converted to succinic acid by incorporation of one atom of oxygen with concomitant decarboxylation  [Pg.94]

HOOC—CH2—CH2—CO-COOH - HOOC—CH2—CH2-COOH + CO2 (X-Ketoglutaric acid Succinic acid [Pg.94]

A similar reaction is catalyzed by 4-hydroxyphenylpyruvate dioxygenase (D 22). The substrate, p-hydroxyphenylpyruvic acid, possesses a keto grouping in the side chain. The oxygen molecule probably reacts first with this carbonyl group under simultaneous decarboxylation. The other oxygen atom is added to [Pg.94]


In nature, vitamin A aldehyde is produced by the oxidative cleavage of P-carotene by 15,15 - P-carotene dioxygenase. Alternatively, retinal is produced by oxidative cleavage of P-carotene to P-apo-S -carotenal followed by cleavage at the 15,15 -double bond to vitamin A aldehyde (47). Carotenoid biosynthesis and fermentation have been extensively studied both ia academic as well as ia iadustrial laboratories. On the commercial side, the focus of these iavestigations has been to iacrease fermentation titers by both classical and recombinant means. [Pg.101]

J Li, MR Nelson, CY Peng, D Bashford, L Noodleman. Incorporating protein environments in density functional theory A self-consistent reaction field calculation of redox potentials of [2Ee2S] clusters in feiTedoxm and phthalate dioxygenase reductase. J Phys Chem A 102 6311-6324, 1998. [Pg.411]

Scheme 10.21 Dioxygenase mechanism of epoxyquinone formation. The 180 isotope labels are omitted for clarity in the lower pathway. Scheme 10.21 Dioxygenase mechanism of epoxyquinone formation. The 180 isotope labels are omitted for clarity in the lower pathway.
Scheme 10.23 Possible dioxygenase mechanism for the transformation of protoasukamycin to asukamycin. Scheme 10.23 Possible dioxygenase mechanism for the transformation of protoasukamycin to asukamycin.
Oxygenases - add one (monooxygenases) or both (dioxygenases) atoms of molecular oxygen to molecules, eg... [Pg.12]

Benzene dioxygenase is a complex enzyme consisting of three protein components, that catalyse the conversion of benzene to benzene cis-dihydrodiol. Give two reasons why this biotransformation should be carried out using whole cells as opposed to using enzyme preparations. [Pg.17]

Pyrocatechol dioxygenases. 6, 325 Pyrocatechol violet metallochromic indicator, 1,556 Pyrogallol... [Pg.206]

Sulfoxidations are not restricted to MOs but can also be carried out by dioxygenases. For example. Pseudomonas mutant strain UV4 producing a toluene dioxygenase (TOO) and Pseudomonas NCIMB 8859 expressing a naphthalene dioxygenase (NDO) were used to oxidize aryl sulfides to antipodal chiral sulfoxides [203]. [Pg.254]

Metabolic pathways containing dioxygenases in wild-type strains are usually related to detoxification processes upon conversion of aromatic xenobiotics to phenols and catechols, which are more readily excreted. Within such pathways, the intermediate chiral cis-diol is rearomatized by a dihydrodiol-dehydrogenase. While this mild route to catechols is also exploited synthetically [221], the chirality is lost. In the context of asymmetric synthesis, such further biotransformations have to be prevented, which was initially realized by using mutant strains deficient in enzymes responsible for the rearomatization. Today, several dioxygenases with complementary substrate profiles are available, as outlined in Table 9.6. Considering the delicate architecture of these enzyme complexes, recombinant whole-cell-mediated biotransformations are the only option for such conversions. E. coli is preferably used as host and fermentation protocols have been optimized [222,223]. [Pg.257]

Benzoate dioxygenase (BZDO) Ralstonia eutropha (former Alcaligenes eutrophus) 1971 [236] [224]... [Pg.258]


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1.2- dihydroxy naphthalene dioxygenase

2,4-Dichlorophenoxyacetate dioxygenase

2-Halobenzoate 1,2-dioxygenases

2-Ketoglutarate dioxygenase

2-Oxoglutarate dioxygenase

2-Oxoglutarate-dependent dioxygenase

2-nitrotoluene-2,3-dioxygenase

2.3- Dihydroxybenzoate 2.3-dioxygenase

2.3- dihydroxybiphenyl 1,2-dioxygenase

3- Hydroxyanthranilate dioxygenase

4-Hydroxyphenyl pyruvate dioxygenase

4-Hydroxyphenylpyruvate dioxygenase HPPD), inhibition

4-Hydroxyphenylpyruvate dioxygenase inhibitors

4-hydroxyphenylpyruvate dioxygenase 4-HPPD)

A High-Valent Fe Intermediate of Tryptophan 2,3-Dioxygenase

A-keto acid-dependent dioxygenase

A-keto acid-dependent dioxygenases

A-ketoglutarate dioxygenases

Acireductone dioxygenase

Activation of HOOH for dioxygenase chemistry

Amino acid tryptophan dioxygenase

Aniline dioxygenase

Anthranilate 1,2-dioxygenase

Application of Aromatic Hydrocarbon Dioxygenases

Arene dioxygenase

Aromatic hydrocarbon dioxygenases

Aromatic hydrocarbon dioxygenases reactions catalyzed

Aryl dioxygenases

Ascorbate dioxygenase

Bacterial dioxygenases

Benzene dioxygenase

Benzene dioxygenases

Benzoate dioxygenase

Biocatalytic Asymmetric Oxidations with Dioxygenases

Biocatalytic with dioxygenases

Biphenyl dioxygenase

Biphenyl dioxygenases

Carotene dioxygenase

Carotenoid cleavage dioxygenase

Carotenoid cleavage dioxygenases

Catalytic taurine dioxygenase

Catechol 2,3-dioxygenase, mechanism-based

Catechol dioxygenase reaction

Catechol dioxygenases

Catechol dioxygenases active site

Catechol dioxygenases iron coordination

Catechol dioxygenases mechanism

Catechol dioxygenases spectroscopy

Catechol dioxygenases structure

Catechol dioxygenases substrate activation

Catechol-1,2-dioxygenase

Chlorobenzene dioxygenase

Chlorocatechol -1,2 -dioxygenase

Chlorocatechol dioxygenases

Cl-catechol 1,2-dioxygenase

Compounds 3- dioxygenase system

Copper dioxygenase

Cysteamine dioxygenase

Cysteamine dioxygenase activity

Cysteine dioxygenase

Dihydroxypyridine dioxygenase

Dinitrotoluene dioxygenase

Dioxygen dioxygenase” type mechanism

Dioxygenase

Dioxygenase activity

Dioxygenase bacterial

Dioxygenase copper complexes

Dioxygenase heme-containing

Dioxygenase mechanisms

Dioxygenase model

Dioxygenase phenolic

Dioxygenase properties

Dioxygenase reactions

Dioxygenase reductase

Dioxygenase regioselectants

Dioxygenase ring-opening

Dioxygenase site-directed mutagenesis

Dioxygenase, enzyme reactions

Dioxygenase-catalyzed oxidations

Dioxygenase-model oxygenations

Dioxygenases 2-ketoglutarate

Dioxygenases 2-oxoglutarate-dependent

Dioxygenases arene dihydroxylation

Dioxygenases aromatic ring

Dioxygenases copper complexes

Dioxygenases cytochrome oxidases

Dioxygenases increased specificity

Dioxygenases non-heme

Dioxygenases ring fission

Dioxygenases three component

Dopa 4,5-dioxygenase

Double bond cleaving dioxygenases

Ene-diol Cleaving Dioxygenases

Enzyme 1- Tryptophan 2,3-dioxygenase

Enzyme 2,4-dioxygenase

Enzyme anthranilate 1,2-dioxygenase

Enzyme catechol 1,2-dioxygenase

Enzyme dioxygenases

Enzymes catechol dioxygenases

External Flavoprotein Dioxygenases

External flavoprotein dioxygenase

Extradiol aromatic dioxygenases

Extradiol cleaving dioxygenases

Extradiol dioxygenases

Extradiol dioxygenases oxygen activation

Extradiol dioxygenases reaction mechanisms

Extradiol ring fission dioxygenases

Ferrous protocatechuate 3,4-dioxygenase

Flavin-containing dioxygenases

Flavoprotein dioxygenases

Gentisate dioxygenase

Gentisate dioxygenases

Glucagon, tryptophan dioxygenase

Heme dioxygenases

Heme dioxygenases catalytic enzymes

Heme dioxygenases reaction mechanism

Heme dioxygenases structure

Heme saturation, tryptophan dioxygenase

Homogentisate 1,2-dioxygenase

Homogentisic dioxygenase

Homoprotocatechuate 2,3-dioxygenase

Human indoleamine 2,3-dioxygenase

Human tryptophan 2,3-dioxygenase

Hydroxy dioxygenase

Hydroxyphenylpyruvate Dioxygenase (HPPD) - the Herbicide Target

Hydroxyphenylpyruvate Dioxygenase (HPPD) Inhibitors Heterocycles

Hydroxyphenylpyruvate dioxygenase

Hydroxyphenylpyruvate dioxygenase HPPD) inhibitors

Indolamine 2,3-dioxygenase

Indole dioxygenase

Indoleamine 2,3-dioxygenase

Indoleamine 2,3-dioxygenase inhibitors

Induction of Tryptophan Dioxygenase by Glucocorticoid Hormones

Inhibition dioxygenase inhibitors

Intradiol aromatic dioxygenases

Intradiol catechol dioxygenase

Intradiol dioxygenases

Intradiol dioxygenases oxygen activation

Intradiol dioxygenases reaction mechanisms

Intradiol dioxygenases structure

Intramolecular dioxygenases

Iron dioxygenases

Leucoanthocyanidin dioxygenase

Leucoanthocyanidin dioxygenase LDOX)

Limited Activity of Carotene Dioxygenase

Linoleic acid dioxygenase

Manganese dioxygenase

NAD tryptophan dioxygenase

Naphthalene dioxygenase

Naphthalene dioxygenases

Nicotinamide tryptophan dioxygenase

Nitrobenzene dioxygenase

Nitropropane dioxygenase

Non-heme iron dioxygenase models

Non-heme iron dioxygenases

Other Double Bond-Cleaving Dioxygenases

Oxidoreductase dioxygenase

Oxygenases dioxygenases

Oxygenases tryptophan 2,3-dioxygenase

P-Carotene 15,15 -dioxygenase

P-hydroxyphenylpyruvate dioxygenase

Peroxidizing dioxygenases

Phenanthrene dioxygenase

Phthalate Dioxygenase Reductase (PDR)

Phthalate dioxygenase

Phthalate dioxygenase reductase

Phthalate dioxygenase reductase, structure

Poly aromatic dioxygenase

Poly dioxygenase

Proline,2-Oxoglutarate Dioxygenases

Protocatechuate 3,4-dioxygenase

Protocatechuate 3,4-dioxygenase mechanism

Protocatechuate 3,4-dioxygenase structure

Protocatechuate extradiol dioxygenase

Protocatechuate intradiol dioxygenase

Pyrazon dioxygenase

Pyridoxate dioxygenase

Pyrimidine deoxynucleotide dioxygenase

Pyrocatechol dioxygenase

Pyrocatechol dioxygenases

Pyruvic oxime dioxygenase

Quercetin 2,5-dioxygenase

Quercetin 2,5-dioxygenase oxidative cleavage

Quercitin dioxygenase

Rat liver cysteine dioxygenase

Rieske dioxygenase

Rieske dioxygenases

Rieske dioxygenases active sites

Rieske dioxygenases structure

Rieske-type proteins dioxygenase

Ring Fission by 2,3-Dihydroxybiphenyl Dioxygenase

Saturation of Tryptophan Dioxygenase with Its Heme Cofactor

Selectivity dioxygenase inhibitors

Steroid dioxygenase

Sulfur dioxygenase

Sulfur oxidizing dioxygenases

Taurine dioxygenase

Taurine, a-ketoglutarate dioxygenase

Taurine, a-ketoglutarate dioxygenase TauD)

Tetrachlorobenzene dioxygenase

The Catechol Dioxygenases

The Reaction Specificity of Carotene Dioxygenase

Thymidine dioxygenase

Thymine dioxygenase

Toluene Dioxygenase Indigo or Prostaglandins from Substituted Benzenes via cis-Dihydrodiols

Toluene dioxygenase

Toluene dioxygenase, biocatalytic

Toluene dioxygenases

Tryptophan decarboxylase dioxygenase

Tryptophan dioxygenase

Tryptophane dioxygenase

Vitamin carotene dioxygenase

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