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Literature summary for 1.1.1.62 extracted from

  • Sawicki, M.W.; Erman, M.; Puranen, T.; Vihko, P.; Ghosh, D.
    Structure of the ternary complex of human 17beta-hydroxysteroid dehydrogenase type 1 with 3-hydroxyestra-1,3,5,7-tetraen-17-one (equilin) and NADP+ (1999), Proc. Natl. Acad. Sci. USA, 96, 840-845.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
medicine binding of equilin at the active site of the enzyme is the basis for inhibition of reduction of estrone to estradiol. One possible outcome of estrogen replacement therapy in vivo can be the reduction of estradiol levels in breast tissues and hence the reduced risk of estrogen-dependent breast cancer Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
ternary complex of the 17beta-hydroxysteroid dehydrogenase type 1 with 3-hydroxyestra-1,3,5,7-tetraen-17-one and NADP+ Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
equilin
-
Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
estrone + NADH Homo sapiens key enzyme responsible for elevated levels of 17beta-estradiol in breast tumor tissues estradiol-17beta + NAD+
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P14061 type 1 enzyme
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
estrone + NADH key enzyme responsible for elevated levels of 17beta-estradiol in breast tumor tissues Homo sapiens estradiol-17beta + NAD+
-
?