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2-oxo-pantoate + NAD+ = 2-oxo-4-dehydropantoate
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2-dehydropantoate + NADH + H+ = (R)-pantoate + NAD+
2-dehydropantoate + NADH + H+ = (R)-pantoate + NAD+
2-dehydropantoate + NADPH + H+ = (R)-pantoate + NADP+
2-dehydropantoate + NADPH + H+ = (R)-pantoate + NADP+
2-dehydropantoate + NADPH = (R)-pantoate + NADP+
2-dehydropantoate + NADPH = (R)-pantoate + NADP+
2-oxopantoate + 3'-NADPH = (R)-pantoate + 3'-NADP+
2-oxopantoate + 3'-NADPH = (R)-pantoate + 3'-NADP+
2-oxopantoate + alpha-NADPH = (R)-pantoate + alpha-NADP+
2-oxopantoate + alpha-NADPH = (R)-pantoate + alpha-NADP+
2-oxopantoate + beta-NADPH = (R)-pantoate + beta-NADP+
2-oxopantoate + beta-NADPH = (R)-pantoate + beta-NADP+
2-oxopantoate + NADPH = (R)-pantoate + NADP+
2-oxopantoate + NADPH = (R)-pantoate + NADP+
2-oxopantoate + thio-NADPH = (R)-pantoate + thio-NADP+
2-oxopantoate + thio-NADPH = (R)-pantoate + thio-NADP+
alpha-ketopantoate + NADPH = D-pantoate + NADP+
alpha-ketopantoate + NADPH = D-pantoate + NADP+
ketopantoate + ? = pantothenate + ?
ketopantoate + ? = pantothenate + ?
ketopantoate + NADPH = pantoate + NADP+
ketopantoate + NADPH = pantoate + NADP+
ketopantoic acid + ? = D-pantoic acid
ketopantoic acid + ? = D-pantoic acid
ketopantoic acid + NADH = pantoic acid + NAD+
ketopantoic acid + NADH = pantoic acid + NAD+
ketopantoic acid + NADPH = D-pantoic acid + NADP+
ketopantoic acid + NADPH = D-pantoic acid + NADP+
ketopantoic acid + NADPH = pantoic acid + NADP+
ketopantoic acid + NADPH = pantoic acid + NADP+
2-oxopantoate + NADH + H+ = ? + NAD+
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2-ketopantoate + NADPH + H+ = ?
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2-oxo-3,3-dimethyl-4-hydroxybutanoate + reduced benzyl viologen = 3,3-dimethyl-2,4-dihydroxybutanoate + oxidized benzyl viologen
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2-oxo-3,3-dimethyl-4-hydroxybutanoate + reduced methyl viologen = 3,3-dimethyl-2,4-dihydroxybutanoate + oxidized methyl viologen
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tetrahydropteroyldiglutamate + 2-dehydropantoate = 5,10-methylenetetrahydropteroyldiglutamate + 3-methyl-2-oxobutanoate + H2O
tetrahydropteroylheptaglutamate + 2-dehydropantoate = 5,10-methylenetetrahydropteroylheptaglutamate + 3-methyl-2-oxobutanoate + H2O
tetrahydropteroylhexaglutamate + 2-dehydropantoate = 5,10-methylenetetrahydropteroylhexaglutamate + 3-methyl-2-oxobutanoate + H2O
tetrahydropteroylpentaglutamate + 2-dehydropantoate = 5,10-methylenetetrahydropteroylpentaglutamate + 3-methyl-2-oxobutanoate + H2O
tetrahydropteroyltetraglutamate + 2-dehydropantoate = 5,10-methylenetetrahydropteroyltetraglutamate + 3-methyl-2-oxobutanoate + H2O
tetrahydropteroyltriglutamate + 2-dehydropantoate = 5,10-methylenetetrahydropteroyltriglutamate + 3-methyl-2-oxobutanoate + H2O
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Ketopantoate formation by a hydroxymethylation enzyme from Escherichia coli
1957
McIntosh, E.N.; Purko, M.; Wood, W.A.
J. Biol. Chem.
228
499-510
The bacterial degradation of pantothenic acid. II. Enzymatic formation of aldopantoic acid
1966
Goodhue, C.T.; Snell, E.E.
Biochemistry
5
403-408
-
Novel enzymic production of D-(-)-pantoyl lactone through the stereospecific reduction of ketopantoic acid
1990
Kataoka, M.; Shimizu, S.; Yamada, H.
Agric. Biol. Chem.
54
177-182
Ketopantoic acid reductase of Pseudomonas maltophilia 845. Purification, characterization, and role in pantothenate biosynthesis
1988
Shimizu, S.; Kataoka, M.; Ching-Ming Chung, M.; Yamada, H.
J. Biol. Chem.
263
12077-12084
-
Separation and preliminary studies on 2-ketopantoyl lactone and 2-ketopantoic acid reductases of yeast
1972
King, H.L.; Wilken, D.R.
J. Biol. Chem.
247
4096-4098
Ketopantoic acid and ketopantoyl lactone reductases. Stereospecificity of transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate
1975
Wilken, D.R.; King, H.L.; Dyar, R.E.
J. Biol. Chem.
250
2311-2314
Pantothenate production in Escherichia coli K12 by enhanced expression of the panE gene encoding ketopantoate reductase
1999
Elischewski, F.; Puhler, A.; Kalinowski, J.
J. Biotechnol.
75
135-146
ApbA, the ketopantoate reductase enzyme of Salmonella typhimurium is required for the synthesis of thiamine via the alternative pyrimidine biosynthetic pathway
1998
Frodyma, M.E.; Downs, D.
J. Biol. Chem.
273
5572-5576
Kinetic and mechanistic analysis of the E. coli panE-encoded ketopantoate reductase
2000
Zheng, R.; Blanchard, J.S.
Biochemistry
39
3708-3717
Identification of active site residues in E. coli ketopantoate reductase by mutagenesis and chemical rescue
2000
Zheng, R.; Blanchard, J.S.
Biochemistry
39
16244-16251
Crystal structure of Escherichia coli ketopantoate reductase at 1.7 A resolution and insight into the enzyme mechanism
2001
Matak-Vinkovic, D.; Vinkovic, M.; Saldanha, S.A.; Ashurst, J.L.; von Delft, F.; Inoue, T.; Miguel, R.N.; Smith, A.G.; Blundell, T.L.; Abell, C.
Biochemistry
40
14493-14500
Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis
1976
Teller, J.H.; Powers, S.G.; Snell, E.E.
J. Biol. Chem.
251
3780-3785
Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties
1976
Powers, S.G.; Snell, E.E.
J. Biol. Chem.
251
3786-3793
Purification and properties of ketopantoate hydroxymethyltransferase
1979
Powers, S.G.; Snell, E.E.
Methods Enzymol.
62
204-209
-
Stereochemistry of 2-oxopantoate formation by oxopantoate hydroxymethyltransferase
1979
Wightman, R.H.
J. Chem. Soc. Chem. Commun.
1979
818-819
-
Stereochemistry of pantoate biosynthesis from 2-ketoisovalerate
1979
Aberhart, D.J.
J. Am. Chem. Soc.
101
1354-1355
-
Steric course of ketopantoate hydroxymethyltransferase in E. coli
1984
Aberhart, D.J.; Russell, D.J.
J. Am. Chem. Soc.
106
4902-4906
Isolation and characterization of Bacillus subtilis mutants blocked in the synthesis of pantothenic acid
1991
Baigori, M.; Grau, R.; Morbidoni, H.R.; de Mendoza, D.
J. Bacteriol.
173
4240-4242
-
Cloning and characterization of the Mycobacterium bovis BCG panB gene encoding ketopantoate hydroxymethyltransferase
2001
Kim, J.K.; Kim, K.D.; Lim, J.S.; Lee, H.G.; Kim, S.J.; Cho, S.H.; Jeong, W.H.; Choe, I.S.; Chung, T.W.; Paik, S.G.; Choe, Y.K.
J. Biochem. Mol. Biol.
34
342-346
Cloning and sequencing of the Escherichia coli panB gene, which encodes ketopantoate hydroxymethyltransferase, and overexpression of the enzyme
1993
Jones, C.E.; Brook, J.M.; Buck, D.; Abell, C.; Smith, A.G.
J. Bacteriol.
175
2125-2130
The Aspergillus nidulans panB gene encodes ketopantoate hydroxymethyltransferase, required for biosynthesis of pantothenate and coenzyme A
1999
Kurtov, D.; Kinghorn, J.R.; Unkles, S.E.
Mol. Gen. Genet.
262
115-120
Elevated levels of ketopantoate hydroxymethyltransferase (PanB) lead to a physiologically significant coenzyme A elevation in Salmonella enterica serovar typhimurium
2002
Rubio, A.; Downs, D.M.
J. Bacteriol.
184
2827-2832
Mycobacterium tuberculosis ketopantoate hydroxymethyltransferase: Tetrahydrofolate-independent hydroxymethyltransferase and enolization reactions with alpha-keto acids
2003
Sugantino, M.; Zheng, R.; Yu, M.; Blanchard, J.S.
Biochemistry
42
191-199
-
On a non-pyridine nucleotide-dependent 2-oxoacid reductase of broad specificity from two Proteus species
1985
Neumann, S.; Simon, H.
FEBS Lett.
167
29-32
Substrate specificity and kinetic isotope effect analysis of the Eschericia coli ketopantoate reductase
2003
Zheng, R.; Blanchard, J.S.
Biochemistry
42
11289-11296
Probing the mechanism of the bifunctional enzyme ketol-acid reductoisomerase by site-directed mutagenesis of the active site
2005
Tyagi, R.; Lee, Y.T.; Guddat, L.W.; Duggleby, R.G.
FEBS J.
272
593-602
Ketopantoate reductase activity is only encoded by ilvC in Corynebacterium glutamicum
2003
Merkamm, M.; Chassagnole, C.; Lindley, N.D.; Guyonvarch, A.
J. Biotechnol.
104
253-260
Biophysical tools to monitor enzyme-ligand interactions of enzymes involved in vitamin biosynthesis
2005
Ciulli, A.; Abell, C.
Biochem. Soc. Trans.
33
767-771
The crystal structure of Escherichia coli ketopantoate reductase with NADP+ bound
2005
Lobley, C.M.; Ciulli, A.; Whitney, H.M.; Williams, G.; Smith, A.G.; Abell, C.; Blundell, T.L.
Biochemistry
44
8930-8939
Probing hot spots at protein-ligand binding sites: a fragment-based approach using biophysical methods
2006
Ciulli, A.; Williams, G.; Smith, A.G.; Blundell, T.L.; Abell, C.
J. Med. Chem.
49
4992-5000
pH-tuneable binding of 2-phospho-ADP-ribose to ketopantoate reductase: a structural and calorimetric study
2007
Ciulli, A.; Lobley, C.M.; Tuck, K.L.; Smith, A.G.; Blundell, T.L.; Abell, C.
Acta Crystallogr. Sect. D
63
171-178
Crystal structure of Escherichia coli ketopantoate reductase in a ternary complex with NADP+ and pantoate bound: substrate recognition, conformational change, and cooperativity
2007
Ciulli, A.; Chirgadze, D.Y.; Smith, A.G.; Blundell, T.L.; Abell, C.
J. Biol. Chem.
282
8487-8497
Identification and characterization of an archaeal ketopantoate reductase and its involvement in regulation of coenzyme A biosynthesis
2013
Tomita, H.; Imanaka, T.; Atomi, H.
Mol. Microbiol.
90
307-321
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
Metabolic engineering of Escherichia coli for D-pantothenic acid production
2019
Zhang, B.; Zhang, X.M.; Wang, W.; Liu, Z.Q.; Zheng, Y.G.
Food Chem.
294
267-275
The ternary complex structure of D-mandelate dehydrogenase with NADH and anilino(oxo)acetate
2017
Furukawa, N.; Miyanaga, A.; Nakajima, M.; Taguchi, H.
Biochem. Biophys. Res. Commun.
486
665-670
Show all BRENDA pathways known for ketopantoate
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