Literature summary for 1.1.1.169 extracted from

Lobley, C.M.; Ciulli, A.; Whitney, H.M.; Williams, G.; Smith, A.G.; Abell, C.; Blundell, T.L.
The crystal structure of Escherichia coli ketopantoate reductase with NADP+ bound (2005), Biochemistry, 44, 8930-8939.

Search for more literature for 1.1.1.169

Cloned(Commentary)

Cloned (Comment)	Organism
gene panE, expression of His6-tagged wild-type and mutant enzymes	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified enzyme with bound NADP+, hanging drop vapour diffusion method, 10-15 mg/ml protein at 4°C is mixed with ketopantoate and NADP+ in a ratio of 5:1 and 2:1, respectively, in 0.1 M sodium acetate, pH 4.0-5.0, with 10%2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 2.1 A resolution, ternary complex modelling	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
D248A	site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain	Escherichia coli
E210A	site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain	Escherichia coli
E256A	site-directed mutagenesis, nearly inactive mutant, 2600fold decreased catalytic efficiency, no complementation of a panE knockout mutant strain	Escherichia coli
K176A	site-directed mutagenesis, nearly inactive mutant, 78000fold decreased catalytic efficiency, no complementation of a panE knockout mutant strain	Escherichia coli
K72A	site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain	Escherichia coli
N98A	site-directed mutagenesis, nearly inactive mutant, 4000fold reduced catalytic efficiency, no complementation of a panE knockout mutant strain	Escherichia coli
S244A	site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics and thermodynamics, wild-type enzyme, overview	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ketopantoate + NADPH	Escherichia coli	the enzyme is involved in pantothenate, i.e. vitamin B5, biosynthesis, which is a precursor for CoA	pantoate + NADP+	-	r

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A9J4	gene panE	-

Purification (Commentary)

Purification (Comment)	Organism
native wild-type enzyme by anion exchange and adsorption chromatography, and gel filtration, recombinant His6-tagged enzyme by nickel affinity chromatography	Escherichia coli

Reaction

Reaction	Comment	Organism	Reaction ID
(R)-pantoate + NADP+ = 2-dehydropantoate + NADPH + H+	molecular catalytic mechanism, substrate and cofactor binding, Asn98, Glu256, and Lys176 are essential, overview	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ketopantoate + NADPH	the enzyme is involved in pantothenate, i.e. vitamin B5, biosynthesis, which is a precursor for CoA	Escherichia coli	pantoate + NADP+	-	r
ketopantoate + NADPH	substrate binding structure and thermodynamics	Escherichia coli	pantoate + NADP+	-	r

Synonyms

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

Cofactor

Cofactor	Comment	Organism	Structure
NADP+	cofactor binding structure and thermodynamics, the cofactor is bound in the active site cleft between the N-terminal Rossmann-fold domain and the C-terminal alpha-helical domain	Escherichia coli
NADPH	cofactor binding structure and thermodynamics	Escherichia coli

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Release 2023.1 (January 2023)