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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.169 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

EC Number Protein Variants Comment Organism
1.1.1.169 E256A site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview Escherichia coli
1.1.1.169 K176A site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview Escherichia coli
1.1.1.169 K72A site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview Escherichia coli
1.1.1.169 N98A site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview Escherichia coli
1.1.1.169 R31A site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview Escherichia coli
1.1.1.169 S244A site-directed mutagenesis, altered steady-state kinetics of the mutant compared to the wild-type enzyme, overview 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 of recombinant wild-type and mutant enzymes, overview Escherichia coli
1.1.1.169 0.007
-
 NADPH pH 7.5, 27°C, wild-type enzyme Escherichia coli
1.1.1.169 0.03
-
 2-dehydropantoate pH 7.5, 27°C, wild-type enzyme 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 2-dehydropantoate + NADPH Escherichia coli an essential step for the biosynthesis of pantothenate, i.e. vitamin B5 (R)-pantoate + NADP+
-
 r

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.169 2-dehydropantoate + NADPH an essential step for the biosynthesis of pantothenate, i.e. vitamin B5 Escherichia coli (R)-pantoate + NADP+
-
 r
1.1.1.169 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

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.169 27
-
 assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.169 25
-
 NADPH pH 7.5, 27°C, wild-type enzyme Escherichia coli
1.1.1.169 25
-
 2-dehydropantoate pH 7.5, 27°C, wild-type enzyme Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.169 7.5
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.169 NADP+
-
 Escherichia coli
1.1.1.169 NADPH
-
 Escherichia coli