(Q33899159)

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Molecular and structural aspects of xenobiotic carbonyl metabolizing enzymes. Role of reductases and dehydrogenases in xenobiotic phase I reactions

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Europe PubMed Central

PubMed publication ID

29 July 2017

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Europe PubMed Central

Molecular and structural aspects of xenobiotic carbonyl metabolizing enzymes. Role of reductases and dehydrogenases in xenobiotic phase I reactions (English)

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Europe PubMed Central

PubMed publication ID

29 July 2017

author name string

Oppermann UC

1

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Europe PubMed Central

PubMed publication ID

29 July 2017

Maser E

2

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Europe PubMed Central

PubMed publication ID

29 July 2017

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publication date

1 April 2000

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Europe PubMed Central

PubMed publication ID

29 July 2017

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Europe PubMed Central

PubMed publication ID

29 July 2017

144

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Europe PubMed Central

PubMed publication ID

29 July 2017

1-3

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Europe PubMed Central

PubMed publication ID

29 July 2017

71-81

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Europe PubMed Central

PubMed publication ID

29 July 2017

Substrate activation in pyridine nucleotide-linked reactions: illustrations from the steroid field

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The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 A resolution

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The catalytic reaction and inhibition mechanism of Drosophila alcohol dehydrogenase: observation of an enzyme-bound NAD-ketone adduct at 1.4 A resolution by X-ray crystallography

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Involvement of alcohol dehydrogenase, short-chain dehydrogenase/reductase, aldehyde dehydrogenase, and cytochrome P450 in the control of retinoid signaling by activation of retinoic acid synthesis

1 reference

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Function of alcohol dehydrogenase and aldehyde dehydrogenase gene families in retinoid signaling

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Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family

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An ethoxyquin-inducible aldehyde reductase from rat liver that metabolizes aflatoxin B1 defines a subfamily of aldo-keto reductases

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Mammalian carbonyl reductases

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Crystal structure of human quinone reductase type 2, a metalloflavoprotein

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Three-dimensional structure of holo 3 alpha,20 beta-hydroxysteroid dehydrogenase: a member of a short-chain dehydrogenase family

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Aldehyde dehydrogenase catalytic mechanism. A proposal

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Three-dimensional structure of rat liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily

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Cloning, sequencing, and enzymatic activity of an inducible aldo-keto reductase from Chinese hamster ovary cells

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Nucleotide and deduced amino acid sequence of a human cDNA (NQO2) corresponding to a second member of the NAD(P)H:quinone oxidoreductase gene family. Extensive polymorphism at the NQO2 gene locus on chromosome 6

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Studies on three reductases which have polycyclic aromatic hydrocarbon quinones as substrates

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A new nomenclature for the aldo-keto reductase superfamily.

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Comparative anatomy of the aldo-keto reductase superfamily

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Structure of betaine aldehyde dehydrogenase at 2.1 A resolution

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7 January 2021

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Short-chain dehydrogenases/reductases (SDR)

1 reference

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SDR and MDR: completed genome sequences show these protein families to be large, of old origin, and of complex nature

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Short-chain dehydrogenases. Proteolysis and chemical modification of prokaryotic 3 alpha/20 beta-hydroxysteroid, insect alcohol and human 15-hydroxyprostaglandin dehydrogenases

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The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction

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The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold

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Xenobiotic carbonyl reduction and physiological steroid oxidoreduction. The pluripotency of several hydroxysteroid dehydrogenases

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Identifiers

10.1016/S0300-483X(99)00192-4

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

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