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5,10-methylenetetrahydrofolate + 2-oxo-4-methylthiobutyrate
tetrahydrofolate + ?
-
about 50% of the activity with 3-methyl-2-oxobutanoate
-
-
?
5,10-methylenetetrahydrofolate + 2-oxobutyrate
?
5,10-methylenetetrahydrofolate + 2-oxobutyrate
tetrahydrofolate + ?
-
about 50% of the activity with 3-methyl-2-oxobutanoate
-
-
?
5,10-methylenetetrahydrofolate + 2-oxopentanoate
?
-
-
-
-
?
5,10-methylenetetrahydrofolate + 2-oxopentanoate
tetrahydrofolate + ?
-
about 30% of the activity with 3-methyl-2-oxobutanoate
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
5,10-methylenetetrahydrofolate + 3-methyl-2-oxopentanoate
?
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxopentanoate
tetrahydrofolate + ?
-
about 65% of the activity with 3-methyl-2-oxobutanoate
-
-
?
5,10-methylenetetrahydrofolate + pyruvate
tetrahydrofolate + ?
-
about 20% of the activity with 3-methyl-2-oxobutanoate
-
-
?
formaldehyde + 3-methyl-2-oxobutanoate
2-dehydropantoate
-
enzyme catalyzes methylenetetrahydrofolate-independent hydroxymethyltransferase reaction between free formaldehyde and alpha-ketoisovalerate, formaldehyde is unlikely to be the natural substrate
-
?
formaldehyde + tetrahydrofolate
methylentetrahydrofolate
tetrahydropteroyldiglutamate + 2-dehydropantoate
5,10-methylenetetrahydropteroyldiglutamate + 3-methyl-2-oxobutanoate + H2O
-
-
-
-
r
tetrahydropteroylheptaglutamate + 2-dehydropantoate
5,10-methylenetetrahydropteroylheptaglutamate + 3-methyl-2-oxobutanoate + H2O
-
-
-
-
r
tetrahydropteroylhexaglutamate + 2-dehydropantoate
5,10-methylenetetrahydropteroylhexaglutamate + 3-methyl-2-oxobutanoate + H2O
-
-
-
-
r
tetrahydropteroylpentaglutamate + 2-dehydropantoate
5,10-methylenetetrahydropteroylpentaglutamate + 3-methyl-2-oxobutanoate + H2O
-
-
-
-
r
tetrahydropteroyltetraglutamate + 2-dehydropantoate
5,10-methylenetetrahydropteroyltetraglutamate + 3-methyl-2-oxobutanoate + H2O
-
-
-
-
r
tetrahydropteroyltriglutamate + 2-dehydropantoate
5,10-methylenetetrahydropteroyltriglutamate + 3-methyl-2-oxobutanoate + H2O
-
-
-
-
r
additional information
?
-
5,10-methylenetetrahydrofolate + 2-oxobutyrate
?
-
-
-
-
?
5,10-methylenetetrahydrofolate + 2-oxobutyrate
?
-
also a good substrate
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
essential for the biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of pantothenate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
-
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
formation of ketopantoate, syn. 2-keto-3,3-dimethyl-4-hydroxybutyrate, tetrahydrofolate-dependent enzyme
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
synthesis of ketopantoate, the following components can replace tetrahydrofolate: tetrahydropteroylmono-, di-, tri-, tetra-, penta-, hexa-, and heptaglutamate, absolute requirement for tetrahydrofolate, only the L-isomer is active
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
forms 2-oxopantoate, syn. 3-hydroxymethyl-3-methyl-2-oxobutanoic acid, from 2-oxoisovalerate with retention of configuration at C-3
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
condensation of alpha-ketoisovalerate with the C-1 donor takes place stereospecifically at C-3 and proceeds in a retention mode at C-3, 5,10-methylenetetrahydrofolate-dependent enzyme
-
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
specificity for alpha-ketoisovalerate is less rigid than for tetrahydrofolate
synthesis of ketopantoate, the following components can replace tetrahydrofolate: tetrahydropteroylmono-, di-, tri-, tetra-, penta-, hexa-, and heptaglutamate, absolute requirement for tetrahydrofolate, only the L-isomer is active
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
inversion of the configuration at C-3 of 2-ketoisovalerate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
enzyme is responsible for catalysis of ketopantoate formation in vivo
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
catalytic activity is regulated by the products of the reaction path of which it is one component
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first step in pantoate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
enzyme may be the rate-limiting reaction in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of pantothenate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
enzyme may be the rate-limiting reaction in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
-
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
-
-
-
-
?
formaldehyde + tetrahydrofolate
methylentetrahydrofolate
-
-
-
?
formaldehyde + tetrahydrofolate
methylentetrahydrofolate
-
-
-
-
?
additional information
?
-
-
no substrates: pyruvate, isovalerate, D- and L-valine, 3-methyl-2-butanone
-
-
?
additional information
?
-
-
enzyme catalyzes deuterium exchange in the methylenetetrahydrofolate-independent enolization of alpha-ketoisovalerate or other alpha-keto acids with decreasing efficiency: alpha-ketoisovalerate, alpha-ketobutyrate, alpha-ketovalerate, pyruvate, alpha-ketomethylthiobutyrate, alpha-ketoisocaproate, stereochemistry, first step in the reaction leading to ketopantoate is the enolization of alpha-ketoisovalerate to form the stabilized carbanion
-
-
?
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5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
essential for the biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of pantothenate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
enzyme is responsible for catalysis of ketopantoate formation in vivo
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
catalytic activity is regulated by the products of the reaction path of which it is one component
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first step in pantoate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
enzyme may be the rate-limiting reaction in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of pantothenate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
enzyme may be the rate-limiting reaction in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
-
-
-
-
?
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Ca2+
-
substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Ca2+
-
Km: 0.27 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Co2+
-
requires Mg2+, Mn2+, Co2+ and Zn2+ are progressively less active
Co2+
-
activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+
Co2+
-
substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Co2+
-
Km: 0.33 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Mg2+
-
activates and is required for activity, 0.1 mM Mg2+ is most active, Mn2+, Ni2+, Co2+ and Zn2+ are progressively less active, restores activity after dialysis
Mg2+
-
requires Mg2+, Mn2+, Co2+ and Zn2+ are progressively less active
Mg2+
-
substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Mg2+
-
Km: 0.61 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Mn2+
-
requires Mg2+, Mn2+, Co2+ and Zn2+ are progressively less active
Mn2+
-
activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+
Ni2+
-
activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+
Ni2+
-
substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Ni2+
-
Km: 0.45 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Zn2+
-
requires Mg2+, Mn2+, Co2+ and Zn2+ are progressively less active
Zn2+
-
activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+
Zn2+
-
substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Zn2+
-
Km: 0.08 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
additional information
-
not activated by Cu2+ and Fe2+
additional information
-
metalloenzyme, inactive in absence of divalent metals, enzyme binds metal ions that assist in the polarization of the carbonyl group and stabilize the enolate anion
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174000
-
recombinant enzyme, gel filtration
255000
-
sedimentation equilibrium
25700
-
10 * 27000, SDS-PAGE, 10 * 25700, amino acid analysis
27000
-
10 * 27000, SDS-PAGE, 10 * 25700, amino acid analysis
28179
-
6 * 28179, calculated from the amino acid sequence and electrospray mass spectrometry, 6 * 29000, recombinant enzyme expressed in Escherichia coli Hfr3000 YA139/pCEJ01, SDS-PAGE
29202
-
recombinant enzyme expressed in Escherichia coli BL21 (DE3): 4 * 29000, SDS-PAGE, 4 * 29202, electrospray ionization/mass spectrometry, 4 * 29366, calculated from the amino acid sequence
29337
-
x * 29337, calculated from the amino acid sequence, x * 35000, recombinant enzyme expressed in Escherichia coli BL21, SDS-PAGE
29366
-
recombinant enzyme expressed in Escherichia coli BL21 (DE3): 4 * 29000, SDS-PAGE, 4 * 29202, electrospray ionization/mass spectrometry, 4 * 29366, calculated from the amino acid sequence
340000
recombinant enzyme expressed in Escherichia coli, gel filtration
35000
-
x * 29337, calculated from the amino acid sequence, x * 35000, recombinant enzyme expressed in Escherichia coli BL21, SDS-PAGE
37700
8 * 37700, calculated from the amino acid sequence, 8 * 40000, recombinant enzyme expressed in Escherichia coli, SDS-PAGE
40000
8 * 37700, calculated from the amino acid sequence, 8 * 40000, recombinant enzyme expressed in Escherichia coli, SDS-PAGE
29000
-
recombinant enzyme expressed in Escherichia coli BL21 (DE3): 4 * 29000, SDS-PAGE, 4 * 29202, electrospray ionization/mass spectrometry, 4 * 29366, calculated from the amino acid sequence
29000
-
6 * 28179, calculated from the amino acid sequence and electrospray mass spectrometry, 6 * 29000, recombinant enzyme expressed in Escherichia coli Hfr3000 YA139/pCEJ01, SDS-PAGE
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Teller, J.H.; Powers, S.G.; Snell, E.E.
Ketopantoate hydroxymethyltransferase. I. Purification and role in pantothenate biosynthesis
J. Biol. Chem.
251
3780-3785
1976
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Powers, S.G.; Snell, E.E.
Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties
J. Biol. Chem.
251
3786-3793
1976
Escherichia coli
brenda
Powers, S.G.; Snell, E.E.
Purification and properties of ketopantoate hydroxymethyltransferase
Methods Enzymol.
62
204-209
1979
Escherichia coli
brenda
Wightman, R.H.
Stereochemistry of 2-oxopantoate formation by oxopantoate hydroxymethyltransferase
J. Chem. Soc. Chem. Commun.
1979
818-819
1979
Escherichia coli
-
brenda
Aberhart, D.J.
Stereochemistry of pantoate biosynthesis from 2-ketoisovalerate
J. Am. Chem. Soc.
101
1354-1355
1979
Escherichia coli
-
brenda
Aberhart, D.J.; Russell, D.J.
Steric course of ketopantoate hydroxymethyltransferase in E. coli
J. Am. Chem. Soc.
106
4902-4906
1984
Escherichia coli
-
brenda
Baigori, M.; Grau, R.; Morbidoni, H.R.; de Mendoza, D.
Isolation and characterization of Bacillus subtilis mutants blocked in the synthesis of pantothenic acid
J. Bacteriol.
173
4240-4242
1991
Bacillus subtilis
brenda
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.
Cloning and characterization of the Mycobacterium bovis BCG panB gene encoding ketopantoate hydroxymethyltransferase
J. Biochem. Mol. Biol.
34
342-346
2001
Mycobacterium tuberculosis, Mycobacterium tuberculosis variant bovis, Mycobacterium tuberculosis KIT 10468
-
brenda
Jones, C.E.; Brook, J.M.; Buck, D.; Abell, C.; Smith, A.G.
Cloning and sequencing of the Escherichia coli panB gene, which encodes ketopantoate hydroxymethyltransferase, and overexpression of the enzyme
J. Bacteriol.
175
2125-2130
1993
Escherichia coli
brenda
Kurtov, D.; Kinghorn, J.R.; Unkles, S.E.
The Aspergillus nidulans panB gene encodes ketopantoate hydroxymethyltransferase, required for biosynthesis of pantothenate and coenzyme A
Mol. Gen. Genet.
262
115-120
1999
Aspergillus nidulans (Q9Y7B6), Aspergillus nidulans
brenda
Rubio, A.; Downs, D.M.
Elevated levels of ketopantoate hydroxymethyltransferase (PanB) lead to a physiologically significant coenzyme A elevation in Salmonella enterica serovar typhimurium
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