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Literature summary for 1.1.1.169 extracted from

  • Tomita, H.; Imanaka, T.; Atomi, H.
    Identification and characterization of an archaeal ketopantoate reductase and its involvement in regulation of coenzyme A biosynthesis (2013), Mol. Microbiol., 90, 307-321.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene TK1968, DNA and amino acid sequence determination and analysis, sequence comparison, recombinant expression in Escherichia coli Thermococcus kodakarensis

Protein Variants

Protein Variants Comment Organism
additional information generation of a gene TK1968 disruption mutant Thermococcus kodakarensis

Inhibitors

Inhibitors Comment Organism Structure
CoA strong inhibition, competitive versus NADH, effect on enzyme kinetics, overview Thermococcus kodakarensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics in both reaction directions Thermococcus kodakarensis
0.00135
-
NADPH recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis
0.003
-
NADH recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis
0.006
-
2-dehydropantoate recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis
0.041
-
NAD+ recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis
0.13
-
(R)-pantoate recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis
2.04
-
(R)-pantoate recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34048
-
2 * 34048, sequence calculation, 2 x 30000, about, recombinant enzyme, SDS-PAGE Thermococcus kodakarensis
60000
-
recombinant enzyme, gel filtration Thermococcus kodakarensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(R)-pantoate + NAD+ Thermococcus kodakarensis
-
2-dehydropantoate + NADH + H+
-
r
(R)-pantoate + NAD+ Thermococcus kodakarensis ATCC BAA-918
-
2-dehydropantoate + NADH + H+
-
r
2-dehydropantoate + NADH + H+ Thermococcus kodakarensis the TK1968 protein displays reductase activity specific for 2-oxopantoate and prefers NADH as the electron donor, distinct to the bacterial/eukaryotic NADPH-dependent enzymes (R)-pantoate + NAD+
-
r
2-dehydropantoate + NADH + H+ Thermococcus kodakarensis ATCC BAA-918 the TK1968 protein displays reductase activity specific for 2-oxopantoate and prefers NADH as the electron donor, distinct to the bacterial/eukaryotic NADPH-dependent enzymes (R)-pantoate + NAD+
-
r

Organism

Organism UniProt Comment Textmining
Thermococcus kodakarensis Q5JGC2 gene TK1968
-
Thermococcus kodakarensis ATCC BAA-918 Q5JGC2 gene TK1968
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli by heat treatment, anion-exchange chromatography, and gel filtration Thermococcus kodakarensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-pantoate + NAD+
-
Thermococcus kodakarensis 2-dehydropantoate + NADH + H+
-
r
(R)-pantoate + NAD+
-
Thermococcus kodakarensis ATCC BAA-918 2-dehydropantoate + NADH + H+
-
r
(R)-pantoate + NADP+
-
Thermococcus kodakarensis 2-dehydropantoate + NADPH + H+
-
r
(R)-pantoate + NADP+
-
Thermococcus kodakarensis ATCC BAA-918 2-dehydropantoate + NADPH + H+
-
r
(S)-pantoate + NAD+ low activity Thermococcus kodakarensis 2-dehydropantoate + NADH + H+
-
r
(S)-pantoate + NADP+ low activity Thermococcus kodakarensis 2-dehydropantoate + NADPH + H+
-
r
2-dehydropantoate + NADH + H+
-
Thermococcus kodakarensis (R)-pantoate + NAD+
-
r
2-dehydropantoate + NADH + H+ the TK1968 protein displays reductase activity specific for 2-oxopantoate and prefers NADH as the electron donor, distinct to the bacterial/eukaryotic NADPH-dependent enzymes Thermococcus kodakarensis (R)-pantoate + NAD+
-
r
2-dehydropantoate + NADH + H+
-
Thermococcus kodakarensis ATCC BAA-918 (R)-pantoate + NAD+
-
r
2-dehydropantoate + NADH + H+ the TK1968 protein displays reductase activity specific for 2-oxopantoate and prefers NADH as the electron donor, distinct to the bacterial/eukaryotic NADPH-dependent enzymes Thermococcus kodakarensis ATCC BAA-918 (R)-pantoate + NAD+
-
r
2-dehydropantoate + NADPH + H+
-
Thermococcus kodakarensis (R)-pantoate + NADP+
-
r
additional information D-pantoate is much more preferred over L-pantoate in the reduction reaction, suggesting that the enzyme generates D-pantoate from 2-oxopantoate in the oxidation reaction Thermococcus kodakarensis ?
-
?
additional information D-pantoate is much more preferred over L-pantoate in the reduction reaction, suggesting that the enzyme generates D-pantoate from 2-oxopantoate in the oxidation reaction Thermococcus kodakarensis ATCC BAA-918 ?
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 34048, sequence calculation, 2 x 30000, about, recombinant enzyme, SDS-PAGE Thermococcus kodakarensis

Synonyms

Synonyms Comment Organism
2-dehydropantoate 2-reductase UniProt Thermococcus kodakarensis
ketopantoate reductase
-
Thermococcus kodakarensis
KPR
-
Thermococcus kodakarensis
Tk-KPR
-
Thermococcus kodakarensis
TK1968 protein
-
Thermococcus kodakarensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
90
-
recombinant enzyme Thermococcus kodakarensis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
50 110 and above, activity range, profile overview Thermococcus kodakarensis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60 90 purified recombinant enzyme, pH 6.4, completely stable at for at least 24 h Thermococcus kodakarensis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.22
-
NADPH recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis
2.41
-
NAD+ recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis
3.17
-
(R)-pantoate recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis
3.8
-
(R)-pantoate recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis
19.7
-
NADH recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis
23.1
-
2-dehydropantoate recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.4
-
recombinant enzyme Thermococcus kodakarensis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Thermococcus kodakarensis
NADH preferred cofactor compared to NADPH Thermococcus kodakarensis
NADP+
-
Thermococcus kodakarensis
NADPH
-
Thermococcus kodakarensis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.000042
-
CoA recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis

General Information

General Information Comment Organism
malfunction gene disruption of gene TK1968results in a strain with growth defects that are complemented by addition of pantoate Thermococcus kodakarensis
metabolism ketopantoate reductase from the hyperthermophilic archaeon Thermococcus kodakarensis catalyses the second step in CoA biosynthesis, the reduction of 2-oxopantoate to pantoate. CoA biosynthesis in the archaeon is regulated by feedback inhibition of enzyme ketopantoate reductase Thermococcus kodakarensis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2
-
(R)-pantoate recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis
29
-
(R)-pantoate recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis
60
-
NAD+ recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis
2220
-
NADPH recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis
3830
-
2-dehydropantoate recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis
6540
-
NADH recombinant enzyme, pH 6.4, 70°C Thermococcus kodakarensis