1.1.1.B3: (S)-specific secondary alcohol dehydrogenase

This is an abbreviated version, for detailed information about (S)-specific secondary alcohol dehydrogenase, go to the full flat file.

Reaction

(S)-R-CHOH-R'
+
NAD+
=
R-CO-R'
+
NADH
+
H+

Synonyms

(S)-1-phenylethanol dehydrogenase, ADH, ADH1, ADH2, ADHTt, carbonyl reductase (NADH, specific for (S)-configuration of alcohol), CRII, More, NAD+-dependent (S)-stereospecific alcohol dehydrogenase, PED, SADH, Scr2, short-chain NAD(H)-dependent alcohol dehydrogenase, SOU1, TtADH

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.B3 (S)-specific secondary alcohol dehydrogenase

Crystallization

Crystallization on EC 1.1.1.B3 - (S)-specific secondary alcohol dehydrogenase

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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure. The substrate binding pocket consists of residues P122, W123, E125, S174, N179, V180, S214, P215, G217, Y218, I223, S224, D225, F226 and V227, with all of the residues lying in the flexible loop regions
-
apo-enzyme and bound to NAD+, at a resolution of 2.1 and 2.4 A, respectively. Enzyme is a tetamer with two types of hydrophobic interfaces. NAD+-binding is associated with a conformational shift of the substrate binding loop from a crystallographically unordered open to a more ordered closed form
-