Literature summary for 1.1.1.62 extracted from

Negri, M.; Recanatini, M.; Hartmann, R.W.
Insights in 17beta-HSD1 enzyme kinetics and ligand binding by dynamic motion investigation (2010), PLoS ONE, 5, e12026.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P14061	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
17beta-estradiol + NAD(P)+ = estrone + NAD(P)H + H+	a structural analysis of available crystal structures is performed and representative conformations are assigned to each step of the putative kinetic mechanism. An essential role played by the backbone and side chain motions, especially of the betaFalphaG-loop, in cofactor and substrate binding is disclosed. A selected-fit mechanism is suggested for 17beta-HSD1, where ligand-binding induces concerted motions of the FG-segment and the C-terminal part guide the enzyme along its preferred catalytic pathway	Homo sapiens	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
estrone + NADPH + H+	-	Homo sapiens	estradiol + NADP+	-	?

Subunits

Subunits	Comment	Organism
homodimer	crystal structure	Homo sapiens

Synonyms

Synonyms	Comment	Organism
17beta-HSD1	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Homo sapiens

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Release 2023.1 (January 2023)