(Q48008397)

English

Molecular cloning, overexpression, and characterization of steroid-inducible 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. A novel member of the short-chain dehydrogenase/reductase superfamily.

scientific article published in November 1998

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scholarly article

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/9812981

Molecular cloning, overexpression, and characterization of steroid-inducible 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. A novel member of the short-chain dehydrogenase/reductase superfamily. (English)

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/9812981

1 reference

based on heuristic

inferred from title

Comamonas testosteroni

object named as

Comamonas testosteroni

1 reference

based on heuristic

inferred from title

author name string

Möbus E

1

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/9812981

Maser E

2

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/9812981

language of work or name

0 references

publication date

1 November 1998

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/9812981

number of pages

9

1 reference

based on heuristic

inferred from page(s)

Journal of Biological Chemistry

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/9812981

273

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/9812981

47

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/9812981

30888-30896

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/9812981

Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases

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Characterization of an estrogen-binding protein in the yeast Candida albicans

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Isolation and characterization of a 50 kDa testosterone-binding protein from Pseudomonas testosteroni

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Mammalian glucocorticoid receptor derivatives enhance transcription in yeast

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The viral erbA oncogene protein, a constitutive repressor in animal cells, is a hormone-regulated activator in yeast

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Prokaryotic 20 beta-hydroxysteroid dehydrogenase is an enzyme of the 'short-chain, non-metalloenzyme' alcohol dehydrogenase type

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Molecular cloning and expression of the beta-hydroxysteroid dehydrogenase gene from Pseudomonas testosteroni

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Testosterone-regulated expression of enzymes involved in steroid and aromatic hydrocarbon catabolism in Comamonas testosteroni

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Characterization of a 3 alpha-hydroxysteroid dehydrogenase/carbonyl reductase from the gram-negative bacterium Comamonas testosteroni.

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Oxidative degradation of testosterone by adaptive enzymes

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Reclassification of Pseudomonas acidovorans den Dooren de Jong 1926 and Pseudomonas testosteroni Marcus and Talalay 1956 as Comamonas acidovorans comb. nov. and Comamonas testosteroni comb. nov., with an Emended Description of the Genus Comamonas

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DNA sequencing with chain-terminating inhibitors

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Confidence Limits on Phylogenies: an Approach using the Bootstrap

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Characteristics of short-chain alcohol dehydrogenases and related enzymes

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Short-chain dehydrogenases/reductases (SDR)

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Structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase at 2.20 A resolution

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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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Crystal structure of rat liver dihydropteridine reductase

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Crystal structures of the binary and ternary complexes of 7 alpha-hydroxysteroid dehydrogenase from Escherichia coli

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Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 A resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family

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Structure and function of steroid dehydrogenases involved in hypertension, fertility, and cancer.

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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

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Endocrine activity of plant-derived compounds: an evolutionary perspective

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Unusual evolution of 11beta- and 17beta-hydroxysteroid and retinol dehydrogenases

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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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Purification and structural characterization of placental NAD(+)-linked 15-hydroxyprostaglandin dehydrogenase. The primary structure reveals the enzyme to belong to the short-chain alcohol dehydrogenase family

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Active site directed mutagenesis of 3 beta/17 beta-hydroxysteroid dehydrogenase establishes differential effects on short-chain dehydrogenase/reductase reactions

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Site-directed mutagenesis of the conserved tyrosine 151 of human placental NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase yields a catalytically inactive enzyme

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Site-specific mutagenesis of Drosophila alcohol dehydrogenase: evidence for involvement of tyrosine-152 and lysine-156 in catalysis

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Cloning and primary structure of murine 11 beta-hydroxysteroid dehydrogenase/microsomal carbonyl reductase

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Cloning, DNA sequencing and expression of (3-17)beta hydroxysteroid dehydrogenase from Pseudomonas testosteroni

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Role of aspartic acid 38 in the cofactor specificity of Drosophila alcohol dehydrogenase

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Antibiotic resistance and enhanced insecticide catabolism as consequences of steroid induction in the gram-negative bacterium Comamonas testosteroni.

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Identifiers

10.1074/JBC.273.47.30888

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/9812981

release_a2ncvyspwjgnvjyy4mor7bjg2i

1 reference

https://api.fatcat.wiki/v0/release/a2ncvyspwjgnvjyy4mor7bjg2i

24 November 2022

based on heuristic

mapped directly with Wikidata item

1 reference

Europe PubMed Central

7 February 2018

http://europepmc.org/abstract/MED/9812981

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