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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.169 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

EC Number Protein Variants Comment Organism
1.1.1.169 D248A site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain Escherichia coli
1.1.1.169 E210A site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain Escherichia coli
1.1.1.169 E256A site-directed mutagenesis, nearly inactive mutant, 2600fold decreased catalytic efficiency, no complementation of a panE knockout mutant strain Escherichia coli
1.1.1.169 K176A site-directed mutagenesis, nearly inactive mutant, 78000fold decreased catalytic efficiency, no complementation of a panE knockout mutant strain Escherichia coli
1.1.1.169 K72A site-directed mutagenesis, unaltered activity compared to the wild-type enzyme, functional complementation of a panE knockout mutant strain Escherichia coli
1.1.1.169 N98A site-directed mutagenesis, nearly inactive mutant, 4000fold reduced catalytic efficiency, no complementation of a panE knockout mutant strain Escherichia coli
1.1.1.169 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]

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.169 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

EC Number Organism UniProt Comment Textmining
1.1.1.169 Escherichia coli P0A9J4 gene panE
-

Purification (Commentary)

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

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.169 (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)

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

Synonyms

EC Number Synonyms Comment Organism
1.1.1.169 ketopantoate reductase
-
 Escherichia coli
1.1.1.169 KPR
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.169 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
1.1.1.169 NADPH cofactor binding structure and thermodynamics Escherichia coli