Literature summary for 1.1.1.169 extracted from

Ciulli, A.; Chirgadze, D.Y.; Smith, A.G.; Blundell, T.L.; Abell, C.
Crystal structure of Escherichia coli ketopantoate reductase in a ternary complex with NADP+ and pantoate bound: substrate recognition, conformational change, and cooperativity (2007), J. Biol. Chem., 282, 8487-8497.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant enzymes	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant His6-tagged enzyme in complex with NADP+ and pantoate, hanging drop vapor-diffusion technique, 20°C, 15-30 mg/ml protein with 2 mM NADP+ and 10 mM pantoate, 0.002 ml of protein solution is mixed with an equal volume of well solution containing 35% v/v dioxane, cryoprotection with 20% v/v 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 2.3 A resolution	Escherichia coli

Crystallization (Comment)

Organism

purified recombinant His6-tagged enzyme in complex with NADP+ and pantoate, hanging drop vapor-diffusion technique, 20°C, 15-30 mg/ml protein with 2 mM NADP+ and 10 mM pantoate, 0.002 ml of protein solution is mixed with an equal volume of well solution containing 35% v/v dioxane, cryoprotection with 20% v/v 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 2.3 A resolution

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
E256A	site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview	Escherichia coli
K176A	site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview	Escherichia coli
K72A	site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview	Escherichia coli
N98A	site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview	Escherichia coli
R31A	site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview	Escherichia coli
S244A	site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
additional information	-	additional information	kinetics of recombinant wild-type and mutant enzymes, overview	Escherichia coli
0.007	-	NADPH	pH 7.5, 27°C, wild-type enzyme	Escherichia coli
0.03	-	2-dehydropantoate	pH 7.5, 27°C, wild-type enzyme	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2-dehydropantoate + NADPH	Escherichia coli	an essential step for the biosynthesis of pantothenate, i.e. vitamin B5	(R)-pantoate + NADP+	-	r

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A9J4	gene panE	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2-dehydropantoate + NADPH	an essential step for the biosynthesis of pantothenate, i.e. vitamin B5	Escherichia coli	(R)-pantoate + NADP+	-	r
2-dehydropantoate + NADPH	substrate and product binding structures, hinge bending between the N- and C-terminal domains is observed, which triggers the switch of the essential Lys176 to form a key hydrogen bond with the C2 hydroxyl of pantoate, pantoate forms additional interactions with conserved residues Ser244, Asn98, and Asn180 and with two conservatively varied residues, Asn194 and Asn241, overview	Escherichia coli	(R)-pantoate + NADP+	-	r

Synonyms

Synonyms	Comment	Organism
ketopantoate reductase	-	Escherichia coli
KPR	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
27	-	assay at	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
25	-	NADPH	pH 7.5, 27°C, wild-type enzyme	Escherichia coli
25	-	2-dehydropantoate	pH 7.5, 27°C, wild-type enzyme	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
NADP+	-	Escherichia coli
NADPH	-	Escherichia coli