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Ligand (R)-4-dehydropantoate Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C6 H1 0 O4
(R)-4-dehydropantoate
HVMPYIKTQSOMHA-BYPYZUCNSA-N
Roles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (2 results)Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(R)-4-dehydropantoate + NADPH + H+ = (R)-pantoate + NADP+
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(R)-4-dehydropantoate + NAD+ = (R)-3,3-dimethylmalate + NADH
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In Vivo Product in Enzyme-catalyzed Reactions (1 result)Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(R)-pantoate + NAD+ = (R)-4-dehydropantoate + NADH
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Substrate in Enzyme-catalyzed Reactions (3 results)
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(R)-4-dehydropantoate + NADPH + H+ = (R)-pantoate + NADP+
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(R)-4-dehydropantoate + NAD+ + H2O = (R)-3,3-dimethylmalate + NADH
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(R)-4-dehydropantoate + NAD+ = (R)-3,3-dimethylmalate + NADH
-
Product in Enzyme-catalyzed Reactions (1 result)
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(R)-pantoate + NAD+ = (R)-4-dehydropantoate + NADH
-
Inhibitor in Enzyme-catalyzed Reactions (2 results)
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Enzyme Kinetic Parameters
kcat Value (Turnover Number) (2 results)
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16.6
-
wild type enzyme, at pH 7.5 and 25°C
18.2
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mutant enzyme A181L, at pH 7.5 and 25°C
KM Value (2 results)
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0.0096
-
wild type enzyme, at pH 7.5 and 25°C
8.1
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mutant enzyme A181L, at pH 7.5 and 25°C
Ki Value (1 result)
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0.27
-
wild type enzyme, at pH 7.5 and 25°C
References & Links Literature References (7)
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Purification of pantoate and dimethylmalate dehydrogenase from Pseudomonas fluorescens UK-1
1978
Mäntsälä, P.
Biochim. Biophys. Acta
526
25-33
The bacterial degradation of pantothenic acid. IV. Enzymatic conversion of aldopantoate to alpha-ketoisovalerate
1966
Magee, P.T.; Snell, E.E.
Biochemistry
5
409-416
Evidence for the importance of cysteine and arginine residues in Pseudomonas fluorescens UK-1 pantoate dehydrogenase
1980
Myöhänen, T.; Mäntsälä, P.
Biochim. Biophys. Acta
614
266-273
The bacterial degradation of pantothenic acid. II. Enzymatic formation of aldopantoic acid
1966
Goodhue, C.T.; Snell, E.E.
Biochemistry
5
403-408
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The regulation of pantothenate degradation during the growth of Pseudomonas fluorescens P2: II. Aldopantoate dehydrogenase
1971
Nurmikko, V.; Mäntsälä, P.; Kuusikko, R.; Niemi, R.
Suom. Kemistil. B
44
244-247
The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase
2013
Miyanaga, A.; Fujisawa, S.; Furukawa, N.; Arai, K.; Nakajima, M.; Taguchi, H.
Biochem. Biophys. Res. Commun.
439
109-114
Evidence of kinetic cooperativity in dimeric ketopantoate reductase from Staphylococcus aureus
2015
Sanchez, J.E.; Gross, P.G.; Goetze, R.W.; Walsh, R.M.; Peeples, W.B.; Wood, Z.A.
Biochemistry
54
3360-3369
Links to other databases for (R)-4-dehydropantoate
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