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

Synonyms

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

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Crystallization

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

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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

Debaryomyces hansenii

740303

Saccharolobus solfataricus

697839

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

uncultured bacterium

685078