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Literature summary extracted from

  • Aikawa, Y.; Nishitani, Y.; Tomita, H.; Atomi, H.; Miki, K.
    Crystal structure of ketopantoate reductase from Thermococcus kodakarensis complexed with NADP(.) (2016), Acta crystallogr. Sect. F, 72, 369-375.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.169 gene TK1968, recombinant coexpression of wild-type and mutant Tk-KPR enzyme dimers carrying a His6-tag and a Strep-tag on each monomer in Escherichia coli Thermococcus kodakarensis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.169 purified recombinant tagged enzyme mutant C84A, hanging drop vapour diffusion method, mixing of 0.001 ml of 10 mg /ml protein in 10 mM Tris-HCl, pH 8.0, 1 mM dithiothreitol, mM NADH, and 1 mM 2-oxopantoate, with 0.001 ml of reservoir solution containing 100 mM sodium acetate, pH 5.5, 10% w/v PEG 3350, 20% v/v 2-propanol, and equilibration against 0.5 ml reservoir solution, at 20°C, 1 week, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement method for modeling Thermococcus kodakarensis

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.169 C84A site-directed mutagenesis Thermococcus kodakarensis
1.1.1.169 W129A site-directed mutagenesis Thermococcus kodakarensis
1.1.1.169 Y60A site-directed mutagenesis Thermococcus kodakarensis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.169 CoA feedback inhibition Thermococcus kodakarensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.169 (R)-pantoate + NADP+ Thermococcus kodakarensis
-
 2-dehydropantoate + NADPH + H+
-
 r
1.1.1.169 (R)-pantoate + NADP+ Thermococcus kodakarensis ATCC BAA-918
-
 2-dehydropantoate + NADPH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.169 Thermococcus kodakarensis Q5JGC2
-
-
1.1.1.169 Thermococcus kodakarensis ATCC BAA-918 Q5JGC2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.169 recombinant wild-type and mutant Tk-KPR enzyme dimers carrying a His6-tag and a Strep-tag on each monomer from Escherichia coli by affinity chromatography Thermococcus kodakarensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.169 (R)-pantoate + NADP+
-
 Thermococcus kodakarensis 2-dehydropantoate + NADPH + H+
-
 r
1.1.1.169 (R)-pantoate + NADP+
-
 Thermococcus kodakarensis ATCC BAA-918 2-dehydropantoate + NADPH + H+
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.169 dimer crystal structure analysis Thermococcus kodakarensis

Synonyms

EC Number Synonyms Comment Organism
1.1.1.169 ketopantoate reductase
-
 Thermococcus kodakarensis
1.1.1.169 KPR
-
 Thermococcus kodakarensis
1.1.1.169 Tk-KPR
-
 Thermococcus kodakarensis
1.1.1.169 TK1968
-
 Thermococcus kodakarensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.169 70
-
 assay at Thermococcus kodakarensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.169 6.4
-
 assay at Thermococcus kodakarensis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.169 NADP+
-
 Thermococcus kodakarensis

General Information

EC Number General Information Comment Organism
1.1.1.169 physiological function ketopantoate reductase catalyzes the NAD(P)H-dependent reduction of 2-oxopantoate which is a step in the biosynthesis of coenzyme A Thermococcus kodakarensis