Literature summary for 1.1.1.2 extracted from

Niefind, K.; Muller, J.; Riebel, B.; Hummel, W.; Schomburg, D.
The crystal structure of R-specific alcohol dehydrogenase from Lactobacillus brevis suggests the structural basis of its metal dependency (2003), J. Mol. Biol., 327, 317-328.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
modelling of NADPH and acetophenone into the active site	Levilactobacillus brevis

Inhibitors

Inhibitors	Comment	Organism	Structure
EDTA	0.5 mM, about 15% residual activity	Levilactobacillus brevis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required, two ions per enzyme tetramer	Levilactobacillus brevis

Organism

Organism	UniProt	Comment	Textmining
Levilactobacillus brevis	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetophenone + NADPH + H+	-	Levilactobacillus brevis	1-phenylethanol + NADP+	-	?
additional information	specific for R-stereoisomers of alcohols	Levilactobacillus brevis	?	-	?

Subunits

Subunits	Comment	Organism
tetramer	crystallization data	Levilactobacillus brevis

Synonyms

Synonyms	Comment	Organism
LB-RADH	-	Levilactobacillus brevis

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Release 2023.1 (January 2023)