000 02282 a2200625 4500
005 20250514222808.0
264 0 _c20050712
008 200507s 0 0 eng d
022 _a0021-9258
024 7 _a10.1074/jbc.M501269200
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aThomas, James L
245 0 0 _aIdentification of key amino acids responsible for the substantially higher affinities of human type 1 3beta-hydroxysteroid dehydrogenase/isomerase (3beta-HSD1) for substrates, coenzymes, and inhibitors relative to human 3beta-HSD2.
_h[electronic resource]
260 _bThe Journal of biological chemistry
_cJun 2005
300 _a21321-8 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, P.H.S.
650 0 4 _a3-Hydroxysteroid Dehydrogenases
_xchemistry
650 0 4 _aAllosteric Site
650 0 4 _aAmino Acid Sequence
650 0 4 _aAndrostenols
_xchemistry
650 0 4 _aAnimals
650 0 4 _aArginine
_xchemistry
650 0 4 _aBaculoviridae
_xmetabolism
650 0 4 _aBlotting, Western
650 0 4 _aCatalysis
650 0 4 _aCatalytic Domain
650 0 4 _aCell Line
650 0 4 _aDNA Primers
_xchemistry
650 0 4 _aDihydrotestosterone
_xanalogs & derivatives
650 0 4 _aDose-Response Relationship, Drug
650 0 4 _aElectrophoresis, Polyacrylamide Gel
650 0 4 _aGlutamine
_xchemistry
650 0 4 _aHistidine
_xchemistry
650 0 4 _aHumans
650 0 4 _aInsecta
650 0 4 _aKinetics
650 0 4 _aModels, Chemical
650 0 4 _aModels, Molecular
650 0 4 _aMolecular Sequence Data
650 0 4 _aMutagenesis, Site-Directed
650 0 4 _aMutation
650 0 4 _aNAD
_xchemistry
650 0 4 _aProtein Binding
650 0 4 _aProtein Conformation
650 0 4 _aSequence Homology, Amino Acid
650 0 4 _aStructure-Activity Relationship
650 0 4 _aSubstrate Specificity
650 0 4 _aTissue Distribution
700 1 _aBoswell, Elizabeth L
700 1 _aScaccia, Launa A
700 1 _aPletnev, Vladimir
700 1 _aUmland, Timothy C
773 0 _tThe Journal of biological chemistry
_gvol. 280
_gno. 22
_gp. 21321-8
856 4 0 _uhttps://doi.org/10.1074/jbc.M501269200
_zAvailable from publisher's website
999 _c15468446
_d15468446