Literature summary for 1.1.1.184 extracted from

Aoki, K.; Tanaka, N.; Ishikura, S.; Araki, N.; Imamura, Y.; Hara, A.; Nakamura, K.T.
Crystallization and preliminary X-ray crystallographic studies of pig heart carbonyl reductase (2006), Acta Crystallogr. Sect. F, 62, 1037-1040.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Sus scrofa
expression in Escherichia coli strain BL21(DE3)	Sus scrofa

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallization to crystal forms I and II in the presence of NADPH. Form I crystals belong to the tetragonal space group P42, and diffract to 1.5 A resolution. Form II crystals belong to the tetragonal space group P41212, and diffract to 2.2 A resolution	Sus scrofa
purified and dialyzed recombinant enzyme complexed with cofactor, 3 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 50 mM NaCl, and 1 mM NADPH, hanging drop vapour diffusion method, 0.002 ml of protein and crystallization solutions are mixed at 20°C, and equilibrated against 0.5 ml reservoir solution, which contains 2.2 M sodium citrate and 20%(v/v) glycerol in 100 mM HEPES buffer, pH 7.5 or 1.4 M ammonium sulfate and 20%(v/v) glycerol in 100 mM MES buffer pH 6.0, resulting in two different tetragonal crystal forms, 1 week, X-ray diffraction structure determination and analysis at 1.5-2.2 A resolution	Sus scrofa

Crystallization (Comment)

Organism

crystallization to crystal forms I and II in the presence of NADPH. Form I crystals belong to the tetragonal space group P42, and diffract to 1.5 A resolution. Form II crystals belong to the tetragonal space group P41212, and diffract to 2.2 A resolution

Sus scrofa

purified and dialyzed recombinant enzyme complexed with cofactor, 3 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 50 mM NaCl, and 1 mM NADPH, hanging drop vapour diffusion method, 0.002 ml of protein and crystallization solutions are mixed at 20°C, and equilibrated against 0.5 ml reservoir solution, which contains 2.2 M sodium citrate and 20%(v/v) glycerol in 100 mM HEPES buffer, pH 7.5 or 1.4 M ammonium sulfate and 20%(v/v) glycerol in 100 mM MES buffer pH 6.0, resulting in two different tetragonal crystal forms, 1 week, X-ray diffraction structure determination and analysis at 1.5-2.2 A resolution

Sus scrofa

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytosol	-	Sus scrofa	5829	-

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
27000	-	x * 27000, SDS-PAGE	Sus scrofa

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, gel filtration, and affinity and hydroxylapatite chromatography, followed by ultrafiltration, the protein easily precipitates at concentraions of above 3.3 mg/ml	Sus scrofa

Source Tissue

Source Tissue	Comment	Organism	Textmining
heart	-	Sus scrofa	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme catalyses the NADPH-linked reduction of a variety of carbonyl compounds to their secondary alcohols	Sus scrofa	?	-	?

Subunits

Subunits	Comment	Organism
?	x * 27000, SDS-PAGE	Sus scrofa

Synonyms

Synonyms	Comment	Organism
CR	-	Sus scrofa
More	the enzyme belongs to the short-chain dehydrogenase/reductase family	Sus scrofa
PHCR	-	Sus scrofa

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	specific for	Sus scrofa

pI Value

Organism	Comment	pI Value Maximum	pI Value
Sus scrofa	calculated	-	9.3
Sus scrofa	isoelectric focusing, recombinant enzyme	-	9.3