Crystal Structures of the Binary and Ternary Complexes of 7α-Hydroxysteroid Dehydrogenase from Escherichia coli,
N Tanaka, T Nonaka, T Tanabe, T Yoshimoto… - Biochemistry, 1996 - ACS Publications
7α-Hydroxysteroid dehydrogenase (7α-HSDH; 1 EC 1.1. 1.159) is an NAD+-dependent
oxidoreductase belonging to the short-chain dehydrogenase/reductase (SDR) 1 family. It …
oxidoreductase belonging to the short-chain dehydrogenase/reductase (SDR) 1 family. It …
Speculations on the subject of alcohol dehydrogenase and its properties in Drosophila and other flies
M Ashburner - Bioessays, 1998 - Wiley Online Library
The alcohol dehydrogenases (ADH) and their genes (Adh) of Drosophila have been much
studied by population and evolutionary biologists. I attempt to put some of these studies into …
studied by population and evolutionary biologists. I attempt to put some of these studies into …
Regulation of estrogen action: role of 17β-hydroxysteroid dehydrogenases
H Peltoketo, P Vihko, R Vihko - Vitamins & Hormones, 1998 - Elsevier
Publisher Summary This chapter elaborates the role of 17β-hydroxysteroid dehydroenases
(17HSD) in the regulation of estrogen action. Proper and relevant steroid hormone influence …
(17HSD) in the regulation of estrogen action. Proper and relevant steroid hormone influence …
The catalytic reaction and inhibition mechanism of Drosophila alcohol dehydrogenase: observation of an enzyme-bound NAD-ketone adduct at 1.4 Å resolution by X …
Drosophila alcohol dehydrogenase (DADH) is an NAD+-dependent enzyme that catalyzes
the oxidation of alcohols to aldehydes/ketones. DADH is the member of the short-chain …
the oxidation of alcohols to aldehydes/ketones. DADH is the member of the short-chain …
The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 Å resolution
Drosophila alcohol dehydrogenase (DADH; EC 1.1. 1.1) is a NAD (H)-dependent
oxidoreductase belonging to the short-chain dehydrogenases/reductases (SDR) family. This …
oxidoreductase belonging to the short-chain dehydrogenases/reductases (SDR) family. This …
Origin of substrate specificity of human and rat 17β-hydroxysteroid dehydrogenase type 1, using chimeric enzymes and site-directed substitutions
T Puranen, M Poutanen, D Ghosh, R Vihko… - …, 1997 - academic.oup.com
Abstract Human 17β-hydroxysteroid dehydrogenase (17-HSD) type 1 predominantly
catalyzes the 17β-reduction of estrone to estradiol. The present results, however, show that …
catalyzes the 17β-reduction of estrone to estradiol. The present results, however, show that …
Characterization of structural and functional properties of human 17β-hydroxysteroid dehydrogenase type 1 using recombinant enzymes and site-directed …
T Puranen, M Poutanen, D Ghosh… - Molecular …, 1997 - academic.oup.com
Abstract Human 17β-hydroxysteroid dehydrogenase (17-HSD) type 1 catalyzes the
conversion of the low activity estrogen, estrone, into highly active estradiol, both in the …
conversion of the low activity estrogen, estrone, into highly active estradiol, both in the …
Identification of key residues for enzymatic carboxylate reduction
H Stolterfoht, G Steinkellner… - Frontiers in …, 2018 - frontiersin.org
Carboxylate reductases (CARs, EC 1.2. 1.30) generate aldehydes from their corresponding
carboxylic acid with high selectivity. Little is known about the structure of CARs and their …
carboxylic acid with high selectivity. Little is known about the structure of CARs and their …
Functional implications of the presenilin dimerization: reconstitution of γ-secretase activity by assembly of a catalytic site at the dimer interface of two catalytically …
S Cervantes, CA Saura, E Pomares… - Journal of Biological …, 2004 - ASBMB
Presenilins are the catalytic components of γ-secretase, an intramembrane-cleaving
protease whose substrates include β-amyloid precursor protein (βAPP) and the Notch …
protease whose substrates include β-amyloid precursor protein (βAPP) and the Notch …
Probing the catalytic mechanism of GDP-4-keto-6-deoxy-d-mannose Epimerase/Reductase by kinetic and crystallographic characterization of site-specific mutants
C Rosano, A Bisso, G Izzo, M Tonetti, L Sturla… - Journal of Molecular …, 2000 - Elsevier
GDP-4-keto-6-deoxy-d-mannose epimerase/reductase is a bifunctional enzyme responsible
for the last step in the biosynthesis of GDP-l-fucose, the substrate of fucosyl transferases …
for the last step in the biosynthesis of GDP-l-fucose, the substrate of fucosyl transferases …