Literature summary for 1.1.1.10 extracted from

Ishikura, S.; Usami, N.; El-Kabbani, O.; Hara, A.
Structural determinant for cold inactivation of rodent L-xylulose reductase (2003), Biochem. Biophys. Res. Commun., 308, 68-72.

Search for more literature for 1.1.1.10

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)	Mus musculus

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure analysis and modelling	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
D238E	site-directed mutagenesis, mutant exists in dimeric form at low temperature like the wild-type enzyme resulting in cold inactivation	Mus musculus
D238E/L242W	site-directed mutagenesis, mutation leads to complete prevention of cold inactivation, mutant exists in tetrameric form at low temperature	Mus musculus
D238E/L242W/T244C	site-directed mutagenesis, double mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature	Mus musculus
L242W	site-directed mutagenesis, mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature	Mus musculus
L242W/T244C	site-directed mutagenesis, double mutation leads to partial prevention of cold inactivation, mutant exists in dimeric and tetrameric form at low temperature	Mus musculus
T244C	site-directed mutagenesis, mutant exists in dimeric form at low temperature like the wild-type enzyme resulting in cold inactivation	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-
Mus musculus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant wild-type and mutant enzymes from Escherichia coli	Mus musculus

Reaction

Reaction	Comment	Organism	Reaction ID
xylitol + NADP+ = L-xylulose + NADPH + H+	enzyme with dual function showing L-xylulose reductase and dicarbonyl reductase activities, it is probably identical with sperm 34 kDa protein P34H and diacetyl reductase, EC 1.1.1.5	Mus musculus	a
xylitol + NADP+ = L-xylulose + NADPH + H+	enzyme with dual function showing L-xylulose reductase and dicarbonyl reductase activities, it is probably identical with sperm 34 kDa protein P34H and diacetyl reductase, EC 1.1.1.5	Homo sapiens	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
diacetyl + NAD(P)H	dicarbonyl reductase activity	Mus musculus	acetoin + NAD(P)+	-	r
diacetyl + NAD(P)H	dicarbonyl reductase activity	Homo sapiens	acetoin + NAD(P)+	-	r
L-xylulose + NADPH + H+	-	Mus musculus	L-xylitol + NADP+	-	r
L-xylulose + NADPH + H+	-	Homo sapiens	L-xylitol + NADP+	-	r

Subunits

Subunits	Comment	Organism
More	the dimeric form is inactive	Mus musculus
tetramer	amino acid residues Trp242, Glu238, Arg203, and Cys244 are important for tetramer formation	Mus musculus
tetramer	amino acid residues Trp242, Glu238, Arg203, and Cys244 are important for tetramer formation	Homo sapiens

Synonyms

Synonyms	Comment	Organism
More	enzyme belongs to the short-chain dehydrogenase/reductase family	Mus musculus
More	enzyme belongs to the short-chain dehydrogenase/reductase family	Homo sapiens
XR	-	Mus musculus
XR	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Mus musculus
25	-	assay at	Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	dissociation into inactive dimers at low temperatures	Mus musculus
additional information	-	stable at low temperatures	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Mus musculus
7	-	assay at	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
NADP+	-	Mus musculus
NADP+	-	Homo sapiens
NADPH	-	Mus musculus
NADPH	-	Homo sapiens

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Release 2023.1 (January 2023)