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Synonyms
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D-pantoate:NAD+ 4-oxidoreductase
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pantoate dehydrogenase
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(R)-pantoate + NAD+ = (R)-4-dehydropantoate + NADH + H+
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(R)-pantoate:NAD+ 4-oxidoreductase
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(R)-pantoate + NAD+
(R)-4-dehydropantoate + NADH
2-oxo-pantoate + NAD+
2-oxo-4-dehydropantoate
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Substrates: -
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(R)-pantoate + NAD+
(R)-4-dehydropantoate + NADH
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Substrates: -
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(R)-pantoate + NAD+
(R)-4-dehydropantoate + NADH
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Substrates: -
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(R)-pantoate + NAD+
(R)-4-dehydropantoate + NADH
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Substrates: -
r
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(R)-pantoate + NAD+
(R)-4-dehydropantoate + NADH
(R)-pantoate + NAD+
(R)-4-dehydropantoate + NADH
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Substrates: -
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(R)-pantoate + NAD+
(R)-4-dehydropantoate + NADH
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Substrates: -
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(R)-pantoate + NAD+
(R)-4-dehydropantoate + NADH
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Substrates: -
r
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NAD+
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5,5'-dithiobis(2-nitrobenzoic acid)
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1 mM, 50% inhibition after 4.6 min, half-inactivation time increases to 7.0 min in the presence of 20 mM D-pantoate
iodacetic acid
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1 mM, 50% inhibition after 14 min, half-inactivation time increases to 29.0 min in the presence of 20 mM D-pantoate, 70% inhibition within 50 min at pH 7.2, 20 mM pantoate decreases inactivation from 70 to 30%
p-chloromercuribenzoate
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0.1 mM, 85% inhibition after 15 min, 200 mM 2-mercaptoethanol restores 70% of enzyme activity within 10 min, 20 mM D-pantoate and 1 mM NAD+ prevent inactivation when added simultaneously
Phenylglyoxal
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5.3 mM, 70% inhibition in borate buffer, 92% inhibition in NaHCO3 buffer within 10 min, complete inactivation after prolonged incubation with phenylglyoxal, NAD+ and D-pantoate increase half-inactivation time from 6 min without substrates to 40 and 17 min respectively
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0.033
D-pantoate
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at pH 10.0
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7 - 10
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linear activity increase
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UK1
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brenda
UK1
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brenda
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brenda
Highest Expressing Human Cell Lines
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24000
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4 * 24000, SDS-PAGE
80000
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ultracentrifugation
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tetramer
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4 * 24000, SDS-PAGE
tetramer
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4 * 24000, SDS-PAGE
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unstable without 2-mercaptoethanol, NAD+ stabilizes to a certain extent, the enzyme is unstable below pH 5.5 and above pH 10.0 even in the presence of NAD+
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-20°C, 2 mM potassium phosphate, pH 7.0, 0.01% EDTA, 1 mM mercaptoethanol, several months, no loss of activity
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50°C, protamine sulfate, calcium phosphate gel, ammonium sulfate, 50°C
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ammonium sulfate, 5'-AMP-Sepharose 4B
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ammonium sulfate, 50°C, gel filtration, hydroxyapatite, 60°C, gel filtration
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Mntsl, P.
Purification of pantoate and dimethylmalate dehydrogenase from Pseudomonas fluorescens UK-1
Biochim. Biophys. Acta
526
25-33
1978
Pseudomonas fluorescens, Pseudomonas fluorescens UK1
brenda
Myhnen, T.; Mntsl, P.
Evidence for the importance of cysteine and arginine residues in Pseudomonas fluorescens UK-1 pantoate dehydrogenase
Biochim. Biophys. Acta
614
266-273
1980
Pseudomonas fluorescens, Pseudomonas fluorescens UK1
brenda
Goodhue, C.T.; Snell, E.E.
The bacterial degradation of pantothenic acid. II. Enzymatic formation of aldopantoic acid
Biochemistry
5
403-408
1966
Pseudomonas sp. P2
brenda
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