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Search results 201 to 206 out of 206 for Hsd17b7

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0.016s

Type

Details

Score

Protein Domain

IPR042829 | HSD17B7/Erg27

Type:

Family

Description:

This entry includes a group of 3-keto-steroid reductases, including 17beta-HSD7 (or HSD17B7) from animals and Erg27 from fungi. 3-keto steroid reductase (in concert with other enzymes) catalyzes NADP-dependent sterol C-4 demethylation, as part of steroid biosynthesis. 3-keto reductase is a classical short-chain dehydrogenase/reductase (SDR), with a well conserved canonical active site tetrad and fairly well conserved characteristic NAD-binding motif [, ]. HSD17B7 is the orthologue of the yeast steroid-3-ketoreductase (Erg27), an enzyme of ergosterol biosynthesis []. HSD17B7 catalyses the conversion of estrone (a 17beta-hydroxysteroid) to the biologically active estradiol [, , ]. Similar to Erg27, it also acts as a 3-ketosteroid reductase [].In humans, predominant expression of 17beta-HSD7 is found not only in reproductive tissues (breast, ovary, placenta) but also in liver and developing brain, principal sites of cholesterol synthesis in keeping with the bifunctional nature of this enzyme [, ].

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Protein

O88736

Organism:	Mus musculus/domesticus
Length:	334
Fragment?:	false

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Protein

Q8C5N9

Organism:	Mus musculus/domesticus
Length:	362
Fragment?:	false

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Publication

22190699 | J:185769

First Author:	Le JA
Year:	2012
Journal:	Biol Reprod
Title:	Generation of mice expressing only the long form of the prolactin receptor reveals that both isoforms of the receptor are required for normal ovarian function.
Volume:	86
Issue:	3
Pages:	86

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Publication

29728128 | J:272136

First Author:	Tu X
Year:	2018
Journal:	Reprod Biol Endocrinol
Title:	The ovarian estrogen synthesis function was impaired in Y123F mouse and partly restored by exogenous FSH supplement.
Volume:	16
Issue:	1
Pages:	44

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Publication

12604213 | -

First Author:	Persson B
Year:	2003
Journal:	Chem Biol Interact
Title:	Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs).
Volume:	143-144

Pages:	271-8

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