Literature summary for 1.1.1.184 extracted from

Kamitori, S.; Iguchi, A.; Ohtaki, A.; Yamada, M.; Kita, K.
X-ray structures of NADPH-dependent carbonyl reductase from Sporobolomyces salmonicolor provide insights into stereoselective reductions of carbonyl compounds (2005), J. Mol. Biol., 352, 551-558.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type enzyme in Escherichia coli strain JM109, and of selenomethionine-CR in Escherichia coli strain B834	Sporidiobolus salmonicolor

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant free wild-type or selenomethionine-labeled enzyme and in complex with NADPH, vapour disffusion method, 30 mg/ml protein in 20 mM Tris-HCl, pH 8.0, against a reservoir solution containing 32% w/v PEG 2000 monomethyl ether, 100 mM ammonium sulfate, and 0.2 M sodium acetate, pH 5.0, with or without 4 mM NADPH, X-ray diffraction structure determination and analysis at 1.8 A and 1.6 A resolution, respectively, structure modeling	Sporidiobolus salmonicolor

Crystallization (Comment)

Organism

purified recombinant free wild-type or selenomethionine-labeled enzyme and in complex with NADPH, vapour disffusion method, 30 mg/ml protein in 20 mM Tris-HCl, pH 8.0, against a reservoir solution containing 32% w/v PEG 2000 monomethyl ether, 100 mM ammonium sulfate, and 0.2 M sodium acetate, pH 5.0, with or without 4 mM NADPH, X-ray diffraction structure determination and analysis at 1.8 A and 1.6 A resolution, respectively, structure modeling

Sporidiobolus salmonicolor

Organism

Organism	UniProt	Comment	Textmining
Sporidiobolus salmonicolor	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant wild-type enzyme from Escherichia coli strain JM109 and recombinant selenomethionine-CR from Escherichia coli strain B834, by ammonium sulfate fractionation, hydrophobic interaction and anion exchange chromatography, and gel filtration	Sporidiobolus salmonicolor

Reaction

Reaction	Comment	Organism	Reaction ID
R-CHOH-R' + NADP+ = R-CO-R' + NADPH + H+	stereoselective enzyme, reaction mechanism and substrate binding model, formation of a hydrophobic channel induced by NADPH binding	Sporidiobolus salmonicolor	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
benzaldehyde + NADPH + H+	-	Sporidiobolus salmonicolor	benzylalcohol + NADP+	-	?
camphorquinone + NADPH + H+	-	Sporidiobolus salmonicolor	?	-	?
ethyl 4-chloro-3-oxobutanoate + NAD(P)H + H+	stereospecific reaction, formation of a hydrophobic channel induced by NADPH binding, structure overview	Sporidiobolus salmonicolor	ethyl (S)-4-chloro-3-hydroxybutanoate + NAD(P)+	optically pure (S)-enantiomer	?

Subunits

Subunits	Comment	Organism
More	SSCR has two domains, an NADPH-binding domain and a substrate-binding domain, structure overview	Sporidiobolus salmonicolor

Synonyms

Synonyms	Comment	Organism
More	the enzyme belongs to the short-chain dehydrogenases/reductases family	Sporidiobolus salmonicolor
SSCR	-	Sporidiobolus salmonicolor

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	dependent on, structure of the NADPH-binding domain and interaction between the enzyme and NADPH, overview	Sporidiobolus salmonicolor