Information on EC 2.1.2.11 - 3-methyl-2-oxobutanoate hydroxymethyltransferase

3-methyl-2-oxobutanoate + benzyloxyethanal + H2O

Substrates: -
Products: -

3-methyl-2-oxobutanoate + D-lactaldehyde + H2O

Substrates: -
Products: -

3-methyl-2-oxobutanoate + ethanal + H2O

Substrates: -
Products: -

3-methyl-2-oxobutanoate + hydroxyethanal + H2O

Substrates: -
Products: -

3-methyl-2-oxobutanoate + L-lactaldehyde + H2O

Substrates: -
Products: -

3-methyl-2-oxobutanoate + methanal + H2O

3-methyl-2-oxopentanoate + methanal + H2O

5,10-methylenetetrahydrofolate + 2-oxo-4-methylthiobutyrate

tetrahydrofolate + ?

Substrates: about 50% of the activity with 3-methyl-2-oxobutanoate
Products: -

5,10-methylenetetrahydrofolate + 2-oxobutyrate

5,10-methylenetetrahydrofolate + 2-oxobutyrate

tetrahydrofolate + ?

Substrates: about 50% of the activity with 3-methyl-2-oxobutanoate
Products: -

5,10-methylenetetrahydrofolate + 2-oxopentanoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 2-oxopentanoate

tetrahydrofolate + ?

Substrates: about 30% of the activity with 3-methyl-2-oxobutanoate
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

30 entries

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

28 entries

5,10-methylenetetrahydrofolate + 3-methyl-2-oxopentanoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxopentanoate

tetrahydrofolate + ?

Substrates: about 65% of the activity with 3-methyl-2-oxobutanoate
Products: -

5,10-methylenetetrahydrofolate + pyruvate

tetrahydrofolate + ?

Substrates: about 20% of the activity with 3-methyl-2-oxobutanoate
Products: -

D-3-ethyl-4-hydroxy-2-oxobutanoate + methanal + H2O

Substrates: -
Products: -

D-3-methyl-4-hydroxy-2-oxobutanoate + methanal + H2O

Substrates: -
Products: -

formaldehyde + 3-methyl-2-oxobutanoate

2-dehydropantoate

Substrates: enzyme catalyzes methylenetetrahydrofolate-independent hydroxymethyltransferase reaction between free formaldehyde and alpha-ketoisovalerate, formaldehyde is unlikely to be the natural substrate
Products: -

formaldehyde + tetrahydrofolate

methylentetrahydrofolate

Substrates: -
Products: -

L-3-ethyl-4-hydroxy-2-oxobutanoate + methanal + H2O

Substrates: -
Products: -

L-3-methyl-4-hydroxy-2-oxobutanoate + methanal + H2O

Substrates: -
Products: -

tetrahydropteroyldiglutamate + 2-dehydropantoate

5,10-methylenetetrahydropteroyldiglutamate + 3-methyl-2-oxobutanoate + H2O

Substrates: -
Products: -

tetrahydropteroylheptaglutamate + 2-dehydropantoate

5,10-methylenetetrahydropteroylheptaglutamate + 3-methyl-2-oxobutanoate + H2O

Substrates: -
Products: -

tetrahydropteroylhexaglutamate + 2-dehydropantoate

5,10-methylenetetrahydropteroylhexaglutamate + 3-methyl-2-oxobutanoate + H2O

Substrates: -
Products: -

tetrahydropteroylpentaglutamate + 2-dehydropantoate

5,10-methylenetetrahydropteroylpentaglutamate + 3-methyl-2-oxobutanoate + H2O

Substrates: -
Products: -

tetrahydropteroyltetraglutamate + 2-dehydropantoate

5,10-methylenetetrahydropteroyltetraglutamate + 3-methyl-2-oxobutanoate + H2O

Substrates: -
Products: -

tetrahydropteroyltriglutamate + 2-dehydropantoate

5,10-methylenetetrahydropteroyltriglutamate + 3-methyl-2-oxobutanoate + H2O

Substrates: -
Products: -

additional information

9 entries

3-ethyl-2-oxopentanoate + methanal + H2O

Substrates: -
Products: -

3-ethyl-2-oxopentanoate + methanal + H2O

Substrates: -
Products: -

3-methyl-2-oxobutanoate + methanal + H2O

Substrates: -
Products: -

3-methyl-2-oxobutanoate + methanal + H2O

Substrates: -
Products: -

3-methyl-2-oxopentanoate + methanal + H2O

Substrates: -
Products: -

3-methyl-2-oxopentanoate + methanal + H2O

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 2-oxobutyrate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 2-oxobutyrate

Substrates: also a good substrate
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: essential for the biosynthesis of coenzyme A
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: biosynthesis of pantothenate
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: formation of ketopantoate, syn. 2-keto-3,3-dimethyl-4-hydroxybutyrate, tetrahydrofolate-dependent enzyme

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: 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

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

485702

Substrates: forms 2-oxopantoate, syn. 3-hydroxymethyl-3-methyl-2-oxobutanoic acid, from 2-oxoisovalerate with retention of configuration at C-3
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: 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
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: specificity for alpha-ketoisovalerate is less rigid than for tetrahydrofolate
Products: 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

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: inversion of the configuration at C-3 of 2-ketoisovalerate
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

485700, 485701, 485704

Substrates: first committed step in pantothenate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: first committed step in pantothenate biosynthesis
Products: enzyme is responsible for catalysis of ketopantoate formation in vivo

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: catalytic activity is regulated by the products of the reaction path of which it is one component
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

485702, 485704

Substrates: biosynthesis of coenzyme A
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: first step in pantoate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: first committed step in pantothenate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: first committed step in pantothenate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: enzyme may be the rate-limiting reaction in pantothenate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: first committed step in pantothenate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: first committed step in pantothenate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: first committed step in pantothenate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: biosynthesis of pantothenate
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Salmonella enterica subsp. enterica serovar Typhimurium

Substrates: enzyme may be the rate-limiting reaction in pantothenate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Salmonella enterica subsp. enterica serovar Typhimurium

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: first committed step in pantothenate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Corynebacterium glutamicum CCUG 27702

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Corynebacterium glutamicum CCUG 27702

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Corynebacterium glutamicum NBRC 12168

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Corynebacterium glutamicum NBRC 12168

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Corynebacterium glutamicum NRRL B-2784

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Corynebacterium glutamicum NRRL B-2784

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

additional information

Substrates: no substrates: pyruvate, isovalerate, D- and L-valine, 3-methyl-2-butanone
Products: -

additional information

Substrates: KPHMT can function as a metal-dependent (Class II) aldolase, catalyzing the aldol addition of 2-oxoacids to methanal and operating under a tetrahydrofolate-independent mechanism. The enzyme is able to catalyze the enolization of the 2-oxoacid via an alpha-proton abstraction and formation of the corresponding stabilized carbanion. This enolate can attack the methylene group of MTHF, resulting in the formation of 2-dehydropantoate, in vivo activity, or eventually on other electrophiles, e.g. aldehydes
Products: -

additional information

Substrates: synthesis of 2-substituted 3-hydroxycarboxylic acid derivatives by the enzyme, method, overview. Enzymatic stereo-selective aldol addition of chemically synthetized 2-oxoacids to formaldehyde catalyzed by two enantio-complementary Type II 2-oxoacid aldolases, 2-keto-3-deoxy-L-rhamnonate aldolase (YfaU, EC 4.1.2.53) fused with maltose binding protein from Escherichia coli, and 3-methyl-2-oxobutanoate hydroxymethyltransferase (KPHMT) and variants thereof. The homochiral 3-substituted 4-hydroxy-2-oxoacids produced are transformed into 2-substituted 3-hydroxycarboxylic ester derivatives by oxidative decarboxylation in the presence of hydrogen peroxide and chemical esterification
Products: -

additional information

Substrates: biocatalytic synthesis of homochiral 2-hydroxy-4-butyrolactone derivatives by tandem aldol addition and carbonyl reduction involving enzyme KPHMT from Escherichia coli, method, overview
Products: -

additional information

Substrates: aldol addition of 3,3-disubstituted 2-oxoacids (1) to diverse aldehydes (2), mediated by KPHMT catalysts, to generate 3,3,3-trisubstituted 2-oxoacids (3) bearing a quaternary stereocenter, substrate specificity and reaction mechanisms of wild-type and mutant enzymes, overview. No activity by wild-type and mutant enzymes with D-3-cyclopropyl-4-hydroxy-2-oxobutanoate and L-3-cyclopropyl-4-hydroxy-2-oxobutanoate plus methanal, and with 2-cyclohexyl-2-oxoacetate and 2-cycloheptyl-2-oxoacetate plus D-lactaldehyde or D-erythrose
Products: -

additional information

additional information

additional information

additional information

Substrates: 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
Products: -

show all columns Go to Natural Substrate Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

16 entries

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

28 entries

additional information

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: essential for the biosynthesis of coenzyme A
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: biosynthesis of pantothenate
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

485700, 485701, 485704

Substrates: first committed step in pantothenate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: first committed step in pantothenate biosynthesis
Products: enzyme is responsible for catalysis of ketopantoate formation in vivo

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: catalytic activity is regulated by the products of the reaction path of which it is one component
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

485702, 485704

Substrates: biosynthesis of coenzyme A
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: first step in pantoate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: first committed step in pantothenate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: first committed step in pantothenate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: enzyme may be the rate-limiting reaction in pantothenate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: first committed step in pantothenate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: first committed step in pantothenate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: first committed step in pantothenate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: biosynthesis of pantothenate
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Salmonella enterica subsp. enterica serovar Typhimurium

Substrates: enzyme may be the rate-limiting reaction in pantothenate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate

tetrahydrofolate + 2-dehydropantoate

Substrates: first committed step in pantothenate biosynthesis
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Corynebacterium glutamicum CCUG 27702

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Corynebacterium glutamicum CCUG 27702

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Corynebacterium glutamicum NBRC 12168

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Corynebacterium glutamicum NBRC 12168

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Corynebacterium glutamicum NRRL B-2784

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Corynebacterium glutamicum NRRL B-2784

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O

tetrahydrofolate + 2-dehydropantoate

Substrates: -
Products: -

additional information

show all columns Go to Cofactor Search

additional information

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

5,10-methenyltetrahydrofolate

dependent on

5,10-methylenetetrahydrofolate

9 entries

tetrahydrofolate

10 entries

additional information

no requirement of pyridoxal 5-phosphate as cofactor

Salmonella enterica subsp. enterica serovar Typhimurium

5,10-methylenetetrahydrofolate

5,10-methylenetetrahydrofolate

485699, 485700, 485701, 485702, 485703, 485707

5,10-methylenetetrahydrofolate

5,10-methylenetetrahydrofolate

5,10-methylenetetrahydrofolate

5,10-methylenetetrahydrofolate

5,10-methylenetetrahydrofolate

5,10-methylenetetrahydrofolate

5,10-methylenetetrahydrofolate as cofactor

5,10-methylenetetrahydrofolate

5,10-methylenetetrahydrofolate-dependent enzyme

Salmonella enterica subsp. enterica serovar Typhimurium

tetrahydrofolate

tetrahydrofolate

485702, 485703, 485704, 485707

tetrahydrofolate

tetrahydrofolate

tetrahydrofolate

tetrahydrofolate

tetrahydrofolate

tetrahydrofolate

requires tetrahydrofolate

tetrahydrofolate

tetrahydrofolate-dependent reaction

tetrahydrofolate

absolute requirement for tetrahydrofolate

show all columns Go to Metals and Ions Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Ca2+

Co2+

Mg2+

Mn2+

Ni2+

Zn2+

additional information

5 entries

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+

activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+

Co2+

requires Mg2+, Mn2+, Co2+ and Zn2+ are progressively less active

Co2+

best metal activator

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+

74% activation

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+

activates

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+

26% activation

Mn2+

activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+

Mn2+

requires Mg2+, Mn2+, Co2+ and Zn2+ are progressively less active

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+

activates, Mg2+ is most active followed by Mn2+, Ni2+, Co2+ and Zn2+

Zn2+

requires Mg2+, Mn2+, Co2+ and Zn2+ are progressively less active

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

the enzyme is metal-dependent

additional information

the enzyme is metal-dependent

additional information

the enzyme is dependent on metals

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

show all columns Go to Inhibitor Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

2-dehydropantoate

the enzyme is regulated by negative feedback inhibition

3-Methyl-2-butanone

5 mM, 27% inhibition

3-methyl-2-oxobutanoate

substrate inhibition

coenzyme A

D-valine

5 mM, 16% inhibition

EDTA

complete inhibition

formaldehyde

Isovalerate

5 mM, 39% inhibition

L-valine

5 mM, 23% inhibition

Pantoate

pantothenate

0.5 mM or above

pantothenic acid

pyruvate

5 mM, 38% inhibition

tetrahydrofolate

additional information

coenzyme A

coenzyme A

above 1 mM

formaldehyde

0.8 mM, partial inhibition

formaldehyde

0.8 mM, partial inhibition; forward reaction

Pantoate

Pantoate

0.05 mM or above

tetrahydrofolate

0.38 mM, partial inhibition

tetrahydrofolate

0.38 mM, partial inhibition; forward reaction

additional information

not inactivated by borohydride reduction in the presence of excess substrates

additional information

not inhibited by methylenetetrahydrofolate, i.e. equimolar formaldehyde and tetrahydrofolate, at concentrations up to 2 mM

Go to Disease Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

DISEASE

TITLE OF PUBLICATION

LINK TO PUBMED

Bacteremia

Comparative Exoproteomics and Host Inflammatory Response in Staphylococcus aureus Skin and Soft Tissue Infections, Bacteremia, and Subclinical Colonization.

25809633

Tuberculosis

Mycobacterium tuberculosis ketopantoate hydroxymethyltransferase: tetrahydrofolate-independent hydroxymethyltransferase and enolization reactions with alpha-keto acids.

12515554

Tuberculosis

The crystal structure of the first enzyme in the pantothenate biosynthetic pathway, ketopantoate hydroxymethyltransferase, from M tuberculosis.

12842039

show all columns Go to KM Value Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

2.9

2-oxobutyrate

2-oxopentanoate

0.24 - 3.49

3-methyl-2-oxobutanoate

4 entries

5.9

3-methyl-2-oxopentanoate

0.82

5,10-methylenetetrahydrofolate

5.9

formaldehyde

0.15 - 0.16

ketopantoate

0.18

tetrahydrofolate

0.25

tetrahydropteroyldiglutamate

0.29

tetrahydropteroylheptaglutamate

0.17

tetrahydropteroylhexaglutamate

0.33

tetrahydropteroylmonoglutamate

0.1

Tetrahydropteroylpentaglutamate

0.1

tetrahydropteroyltetraglutamate

0.18

tetrahydropteroyltriglutamate

additional information

0.24

3-methyl-2-oxobutanoate

1.1

3-methyl-2-oxobutanoate

3.13

3-methyl-2-oxobutanoate

pH 6.8, 37°C, recombinant mutant K25A/E189S

3.49

3-methyl-2-oxobutanoate

pH 6.8, 37°C, recombinant wild-type enzyme

5.9

formaldehyde

5.9

formaldehyde

methylenetetrahydrofolate: formaldehyde + tetrahydrofolate

0.15

ketopantoate

0.16

ketopantoate

0.18

tetrahydrofolate

0.18

tetrahydrofolate

forward and reverse reaction, methylenetetrahydrofolate: formaldehyde + tetrahydrofolate

additional information

additional information

low Km-values for its substrates

show all columns Go to Turnover Number Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.43 - 1.16

3-methyl-2-oxobutanoate

4 entries

0.78

5,10-methylenetetrahydrofolate

0.43

3-methyl-2-oxobutanoate

pH 6.8, 37°C, recombinant wild-type enzyme

0.78

3-methyl-2-oxobutanoate

0.783

3-methyl-2-oxobutanoate

1.16

3-methyl-2-oxobutanoate

pH 6.8, 37°C, recombinant mutant K25A/E189S

show all columns Go to kcat/KM Value Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

kcat/KM VALUE [1/mMs^-1]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.12 - 0.37

3-methyl-2-oxobutanoate

0.12

3-methyl-2-oxobutanoate

pH 6.8, 37°C, recombinant wild-type enzyme

0.37

3-methyl-2-oxobutanoate

pH 6.8, 37°C, recombinant mutant K25A/E189S

show all columns Go to Specific Activity Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.0025

strain BD170

0.00254

strain UR1

0.00258

strain UR4

0.00262

strain 168

0.007

strain K12

0.01 - 0.027

recombinant enzyme expressed in Escherichia coli

0.019

recombinant enzyme

0.162

strain Hfr3000 YA139/pCEJ02

0.348

strain Hfr3000 YA139/pCEJ01

0.666

strain Hfr3000 YA139/pSAL38

3890

show all columns Go to pH Optimum Search

purified recombinant enzyme from strain Hfr3000 YA139/pCEJ01

7.3

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

7 - 7.5

7 - 7.6

7.5

assay at

at or below

additional information

assay at

wild-type enzyme and mutant K25A/E189S

7 - 7.5

rate of substrate enolization is pH-dependent with optimal activity in the range of

7 - 7.5

additional information

pI: 4.4

additional information

pI: 4.4

show all columns Go to pH Range Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

no ketopantoate formation above pH 10

5 - 9

about 50% of activity maximum at pH 6 and 9, inactive below pH 5

additional information

stable and active over a broad pH-range

show all columns Go to Temperature Optimum Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at room temperature

7 entries

wild-type enzyme and mutant K25A/E189S

70 - 80

reverse reaction, activity decreases rapidly above 80°C

assay at

assay at

assay at

assay at

assay at

assay at

Salmonella enterica subsp. enterica serovar Typhimurium

assay at

show all columns Go to Organism Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

wild-type strains biA1 and yA2, strain G1765

Uniprot

brenda

strains 168, BD170, UR1, UR4

brenda

SwissProt

brenda

SwissProt

brenda

Corynebacterium glutamicum CCUG 27702

SwissProt

brenda

SwissProt

brenda

SwissProt

brenda

SwissProt

brenda

Corynebacterium glutamicum NBRC 12168

SwissProt

brenda

SwissProt

brenda

Corynebacterium glutamicum NRRL B-2784

SwissProt

brenda

6 entries

776261, 776367, 777922

Uniprot

brenda

brenda

brenda

BCG, strain 1173-P2, live vaccine against tuberculosis, used for superficial bladder cancer immunotherapy

brenda

genomic gene panB, and a second putative MOHMT enzyme, RHE_PE00443, similar to the product of panB, is encoded on plasmid p42e

brenda

genomic gene panB, and a second putative MOHMT enzyme, RHE_PE00443, similar to the product of panB, is encoded on plasmid p42e

brenda

serovar typhimurium

Salmonella enterica subsp. enterica serovar Typhimurium

brenda

brenda

brenda

SwissProt

brenda

brenda

SwissProt

brenda

485699, 485700, 485701, 485702, 485707

brenda

659030

Uniprot

brenda

660518, 756787

brenda

776261, 776367, 777922

Uniprot

brenda

strain ATCC 23783

brenda

strains W and B

brenda

brenda

enzyme is degraded by the proteasome. Maintenance of the physiological levels of 3-methyl-2-oxobutanoate hydroxymethyltransferase and of malonyl-CoA acyl carrier protein transacylase requires Mycobacterium proteasomal ATPase and proteasome accessory factor in addition to proteasome protease activity

673328

brenda

show all columns Go to Localization Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

3 entries

brenda

brenda

most of recombinant enzyme is found in a soluble fraction

brenda

top hide

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

show all columns Go to General Information Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

evolution

metabolism

17 entries

additional information

24 entries

evolution

phylogenetic analysis of rhizobial panCB genes indicates a common origin of chromosomal and plasmid-borne sequences. Gene pan B in Rhizobiales with multipartite genomes, overview

evolution

phylogenetic analysis of rhizobial panCB genes indicates a common origin of chromosomal and plasmid-borne sequences. Gene pan B in Rhizobiales with multipartite genomes, overview

metabolism

the enzyme is the first enzyme of the pantothenate biosynthesis pathway, responsible for the formation of 2-oxopantoate by the transfer of a methyl group from 5,10-methylentetrahydrofolate to 2-oxoisovalerate

metabolism

enzyme overexpression leads to accumulation of the likely folate cleavage product 6-hydroxymethylpterin and other pterins in cells and medium, and to a 46% increase in total folate content

metabolism

the enzyme is involved in D-pantothenic acid biosynthesis

metabolism

the enzyme is regulated by negative feedback inhibition

metabolism

the enzyme is involved in D-pantothenic acid biosynthesis

metabolism

the enzyme is regulated by negative feedback inhibition

metabolism

metabolism

the enzyme is regulated by negative feedback inhibition

metabolism

the enzyme is regulated by negative feedback inhibition

metabolism

the enzyme is regulated by negative feedback inhibition

metabolism

the enzyme is regulated by negative feedback inhibition

metabolism

enzyme overexpression leads to accumulation of the likely folate cleavage product 6-hydroxymethylpterin and other pterins in cells and medium, and to a 46% increase in total folate content

metabolism

the enzyme is regulated by negative feedback inhibition

metabolism

Corynebacterium glutamicum CCUG 27702

the enzyme is regulated by negative feedback inhibition

metabolism

Corynebacterium glutamicum NBRC 12168

the enzyme is regulated by negative feedback inhibition

metabolism

Corynebacterium glutamicum NRRL B-2784

the enzyme is regulated by negative feedback inhibition

metabolism

the enzyme is regulated by negative feedback inhibition

additional information

the putative MOHMT encoded by RHE_PE00443 is not functional under the conditions studied and provides evidence of functional cooperation between p42f and chromosomally encoded proteins for pantothenate biosynthesis

additional information

enzyme structure homology modeling using the Bacillus subtilis KPHMT (PDB ID 1OY0) structure as template. Conformational stability investigations

additional information

structural analysis of enzyme mutant K25A/E189S reveals the expansion of the entry channel and the change of the electric charge from negative to uncharged due to the substitution from glutamic acid to serine at site 189. Molecular docking and structure analysis using Mycobacterium tuberculosis KPHMT (PDB ID 1OY0) as a template. The KPHMT structure reveals a typical (beta/alpha)8 barrel fold, and the docking result provides 15 reference residues in the catalytic pocket of CgKPHMT named Zone 1 that interact with substrate 3-methyl-2-oxobutanoate during catalysis, including T30, Y32, L49, G51, D52, S53, D91, K121, E123, H145, V187, E189, I210, V220, V222

additional information

enzyme structure homology modeling using the Bacillus subtilis KPHMT (PDB ID 1OY0) structure as template. Conformational stability investigations

additional information

additional information

additional information

enzyme structure homology modeling using the Bacillus subtilis KPHMT (PDB ID 1OY0) structure as template. Conformational stability investigations

additional information

additional information

enzyme structure homology modeling using the Bacillus subtilis KPHMT (PDB ID 1OY0) structure as template. Conformational stability investigations

additional information

additional information

enzyme structure homology modeling using the Bacillus subtilis KPHMT (PDB ID 1OY0) structure as template. Conformational stability investigations

additional information

additional information

enzyme structure homology modeling using the Bacillus subtilis KPHMT (PDB ID 1OY0) structure as template. Conformational stability investigations

additional information

additional information

enzyme structure homology modeling using the Bacillus subtilis KPHMT (PDB ID 1OY0) structure as template. Conformational stability investigations

additional information

additional information

Corynebacterium glutamicum CCUG 27702

enzyme structure homology modeling using the Bacillus subtilis KPHMT (PDB ID 1OY0) structure as template. Conformational stability investigations

additional information

Corynebacterium glutamicum CCUG 27702

additional information

Corynebacterium glutamicum NBRC 12168

enzyme structure homology modeling using the Bacillus subtilis KPHMT (PDB ID 1OY0) structure as template. Conformational stability investigations

additional information

Corynebacterium glutamicum NBRC 12168

additional information

Corynebacterium glutamicum NRRL B-2784

enzyme structure homology modeling using the Bacillus subtilis KPHMT (PDB ID 1OY0) structure as template. Conformational stability investigations

additional information

Corynebacterium glutamicum NRRL B-2784

additional information

enzyme structure homology modeling using the Bacillus subtilis KPHMT (PDB ID 1OY0) structure as template. Conformational stability investigations

additional information

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

Show AA Sequence and Transmembrane Helices (20085 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.

Go to PDB and Structure Links Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

PDB

SCOP

CATH

UNIPROT

ORGANISM

Burkholderia pseudomallei

Burkholderia thailandensis E264

Neisseria meningitidis serogroup B

Neisseria meningitidis serogroup B

Neisseria meningitidis serogroup B

show all columns Go to Molecular Weight Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

120000

gel filtration

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

285000

gel filtration

29000

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

show all columns Go to Subunit Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

x * 29337, calculated from the amino acid sequence, x * 35000, recombinant enzyme expressed in Escherichia coli BL21, SDS-PAGE

decamer

12 entries

hexamer

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

octamer

8 * 37700, calculated from the amino acid sequence, 8 * 40000, recombinant enzyme expressed in Escherichia coli, SDS-PAGE

tetramer

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

additional information

673328

decamer

pentamer of dimers, three-dimensional structure modelling, overview

decamer

pentamer of dimers, three-dimensional structure modelling, overview

decamer

pentamer of dimers, three-dimensional structure modelling, overview

decamer

pentamer of dimers, three-dimensional structure modelling, overview

decamer

Corynebacterium glutamicum CCUG 27702

pentamer of dimers, three-dimensional structure modelling, overview

decamer

pentamer of dimers, three-dimensional structure modelling, overview

decamer

pentamer of dimers, three-dimensional structure modelling, overview

decamer

pentamer of dimers, three-dimensional structure modelling, overview

decamer

Corynebacterium glutamicum NBRC 12168

pentamer of dimers, three-dimensional structure modelling, overview

decamer

pentamer of dimers, three-dimensional structure modelling, overview

decamer

Corynebacterium glutamicum NRRL B-2784

pentamer of dimers, three-dimensional structure modelling, overview

decamer

10 * 27000, SDS-PAGE, 10 * 25700, amino acid analysis

show all columns Go to Posttranslational Modification Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

no modification

Go to Crystallization (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

comparative analysis of the Escherichia coli ketopantoate hydroxymethyltransferase crystal structure confirms that it is a member of the (betaalpha)8 phosphoenolpyruvate/pyruvate superfamily

659030

hanging drop vapor diffusion, crystal structure at 1.9 A resolution in complex with its product ketopantoate, the enzyme adopts the (betaalpha)8 barrel fold and the active site contains a ketopantoate bidentately coordiated to Mg2+

660518

show all columns Go to Protein Variants Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

A185S

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

A19N

site-directed mutagenesis, the mutant shows about 20% decreased activity compared to wild-type enzyme

D52A

site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type enzyme

D91A

site-directed mutagenesis, the mutant shows decreased activity compared to wild-type enzyme

E123A

site-directed mutagenesis, the mutant shows decreased activity compared to wild-type enzyme

E189A

site-directed mutagenesis, the mutant shows about 20% increased activity compared to wild-type enzyme

G23A

site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme

G51A

site-directed mutagenesis, the mutant shows decreased activity compared to wild-type enzyme

G95C

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

G95C/E98D

site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type enzyme

H145A

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

H159A

site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme

I210A

site-directed mutagenesis, the mutant shows about 30% decreased activity compared to wild-type enzyme

K121A

site-directed mutagenesis, the mutant shows decreased activity compared to wild-type enzyme

K20A

site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type enzyme

K25A

site-directed mutagenesis, the mutant shows about 2.2fold increased activity compared to wild-type enzyme

K25A/E189S

K25A/E189S/E106S

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability compared to wild-type enzyme, the mutant shows reduced activity compared to wild-type enzyme

K25A/E189S/E106S/S247D

site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme

K25A/E189S/E106S/S247I

site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme

K25A/E189S/E98N

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98N/E106S

site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme

K25A/E189S/E98N/E106S/S247D

site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type enzyme

K25A/E189S/E98N/E106S/S247I

site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme

K25A/E189S/E98N/S247D

site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme, molecular dynamics simulation and structural analysis, residue interactions in the interface of the mutant (M8)

K25A/E189S/E98N/S247I

site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme

K25A/E189S/E98Q

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98T

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98T/E106S

site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme

K25A/E189S/E98T/E106S/S247D

site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme

K25A/E189S/E98T/E106S/S247I

site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme, the mutant shows increased activity compared to wild-type enzyme

K25A/E189S/E98T/S247D

site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme

K25A/E189S/E98T/S247I

site-directed mutagenesis, similar activity compared to wild-type enzyme

K25A/E189S/S247D

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability compared to wild-type enzyme, the mutant shows reduced activity compared to wild-type enzyme

K25A/E189S/S247I

site-directed mutagenesis, interface residue mutation, the mutant shows reduced thermal stability compared to wild-type enzyme

K84A

site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme

L48I

site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type enzyme

L49A

L59F/R61F

site-directed mutagenesis, the mutant shows about 30% decreased activity compared to wild-type enzyme

M47I

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

N214A

site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme

Q24A

site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme

R134M/A138S

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

S27A

site-directed mutagenesis, the mutant shows about 50% increased activity compared to wild-type enzyme

S53A

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

T115A

site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme

T13A

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

T30A

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

T96A

site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme

V187A

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

V21E

site-directed mutagenesis, the mutant shows about 20% increased activity compared to wild-type enzyme

V220A

site-directed mutagenesis, the mutant shows decreased activity compared to wild-type enzyme

V222A

site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type enzyme

V26N

site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type enzyme

V28F

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

V89I

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

Y32A

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

A19N

site-directed mutagenesis, the mutant shows about 20% decreased activity compared to wild-type enzyme

K20A

site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type enzyme

K25A

site-directed mutagenesis, the mutant shows about 2.2fold increased activity compared to wild-type enzyme

K25A/E189S

K25A/E189S/E106S

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability compared to wild-type enzyme, the mutant shows reduced activity compared to wild-type enzyme

K25A/E189S/E98N

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98Q

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98T

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

T13A

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

A19N

site-directed mutagenesis, the mutant shows about 20% decreased activity compared to wild-type enzyme

K20A

site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type enzyme

K25A

site-directed mutagenesis, the mutant shows about 2.2fold increased activity compared to wild-type enzyme

K25A/E189S

K25A/E189S/E106S

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability compared to wild-type enzyme, the mutant shows reduced activity compared to wild-type enzyme

K25A/E189S/E98N

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98Q

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98T

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

T13A

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

A19N

site-directed mutagenesis, the mutant shows about 20% decreased activity compared to wild-type enzyme

K20A

site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type enzyme

K25A

site-directed mutagenesis, the mutant shows about 2.2fold increased activity compared to wild-type enzyme

K25A/E189S

K25A/E189S/E106S

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability compared to wild-type enzyme, the mutant shows reduced activity compared to wild-type enzyme

K25A/E189S/E98N

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98Q

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98T

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

T13A

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

A19N

Corynebacterium glutamicum CCUG 27702

site-directed mutagenesis, the mutant shows about 20% decreased activity compared to wild-type enzyme

K20A

Corynebacterium glutamicum CCUG 27702

site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type enzyme

K25A

Corynebacterium glutamicum CCUG 27702

site-directed mutagenesis, the mutant shows about 2.2fold increased activity compared to wild-type enzyme

K25A/E189S

K25A/E189S/E106S

Corynebacterium glutamicum CCUG 27702

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability compared to wild-type enzyme, the mutant shows reduced activity compared to wild-type enzyme

K25A/E189S/E98N

Corynebacterium glutamicum CCUG 27702

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98Q

Corynebacterium glutamicum CCUG 27702

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98T

Corynebacterium glutamicum CCUG 27702

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

T13A

Corynebacterium glutamicum CCUG 27702

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

A19N

site-directed mutagenesis, the mutant shows about 20% decreased activity compared to wild-type enzyme

K20A

site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type enzyme

K25A

site-directed mutagenesis, the mutant shows about 2.2fold increased activity compared to wild-type enzyme

K25A/E189S

K25A/E189S/E106S

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability compared to wild-type enzyme, the mutant shows reduced activity compared to wild-type enzyme

K25A/E189S/E98N

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98Q

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98T

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

T13A

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

A19N

site-directed mutagenesis, the mutant shows about 20% decreased activity compared to wild-type enzyme

K20A

site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type enzyme

K25A

site-directed mutagenesis, the mutant shows about 2.2fold increased activity compared to wild-type enzyme

K25A/E189S

K25A/E189S/E106S

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability compared to wild-type enzyme, the mutant shows reduced activity compared to wild-type enzyme

K25A/E189S/E98N

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98Q

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98T

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

T13A

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

A19N

site-directed mutagenesis, the mutant shows about 20% decreased activity compared to wild-type enzyme

K20A

site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type enzyme

K25A

site-directed mutagenesis, the mutant shows about 2.2fold increased activity compared to wild-type enzyme

K25A/E189S

K25A/E189S/E106S

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability compared to wild-type enzyme, the mutant shows reduced activity compared to wild-type enzyme

K25A/E189S/E98N

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98Q

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98T

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

T13A

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

A19N

Corynebacterium glutamicum NBRC 12168

site-directed mutagenesis, the mutant shows about 20% decreased activity compared to wild-type enzyme

K20A

Corynebacterium glutamicum NBRC 12168

site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type enzyme

K25A

Corynebacterium glutamicum NBRC 12168

site-directed mutagenesis, the mutant shows about 2.2fold increased activity compared to wild-type enzyme

K25A/E189S

K25A/E189S/E106S

Corynebacterium glutamicum NBRC 12168

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability compared to wild-type enzyme, the mutant shows reduced activity compared to wild-type enzyme

K25A/E189S/E98N

Corynebacterium glutamicum NBRC 12168

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98Q

Corynebacterium glutamicum NBRC 12168

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98T

Corynebacterium glutamicum NBRC 12168

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

T13A

Corynebacterium glutamicum NBRC 12168

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

A19N

site-directed mutagenesis, the mutant shows about 20% decreased activity compared to wild-type enzyme

K20A

site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type enzyme

K25A

site-directed mutagenesis, the mutant shows about 2.2fold increased activity compared to wild-type enzyme

K25A/E189S

K25A/E189S/E106S

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability compared to wild-type enzyme, the mutant shows reduced activity compared to wild-type enzyme

K25A/E189S/E98N

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98Q

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98T

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

T13A

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

A19N

Corynebacterium glutamicum NRRL B-2784

site-directed mutagenesis, the mutant shows about 20% decreased activity compared to wild-type enzyme

K20A

Corynebacterium glutamicum NRRL B-2784

site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type enzyme

K25A

Corynebacterium glutamicum NRRL B-2784

site-directed mutagenesis, the mutant shows about 2.2fold increased activity compared to wild-type enzyme

K25A/E189S

K25A/E189S/E106S

Corynebacterium glutamicum NRRL B-2784

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability compared to wild-type enzyme, the mutant shows reduced activity compared to wild-type enzyme

K25A/E189S/E98N

Corynebacterium glutamicum NRRL B-2784

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98Q

Corynebacterium glutamicum NRRL B-2784

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

K25A/E189S/E98T

Corynebacterium glutamicum NRRL B-2784

site-directed mutagenesis, interface residue mutation, the mutant shows improved thermal stability and similar activity compared to wild-type enzyme

T13A

Corynebacterium glutamicum NRRL B-2784

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

I202A

site-directed mutagenesis, the mutant tolerates 3-monosubstituted 2-oxoacids with linear, branched, or cyclic substituents, mutant substrate specificity compared to wild-type, overview

I202A/I212A

site-directed mutagenesis, mutant substrate specificity compared to wild-type, overview

I202A/I212A/V214G

site-directed mutagenesis, mutant substrate specificity compared to wild-type, overview

I202A/V214G

site-directed mutagenesis, mutant substrate specificity compared to wild-type, overview

I212A

I212A/V214G

site-directed mutagenesis, mutant substrate specificity compared to wild-type, overview

V214G

site-directed mutagenesis, mutant substrate specificity compared to wild-type, overview

I202A

site-directed mutagenesis, the mutant tolerates 3-monosubstituted 2-oxoacids with linear, branched, or cyclic substituents, mutant substrate specificity compared to wild-type, overview

I202A/I212A

site-directed mutagenesis, mutant substrate specificity compared to wild-type, overview

I202A/V214G

site-directed mutagenesis, mutant substrate specificity compared to wild-type, overview

I212A

V214G

site-directed mutagenesis, mutant substrate specificity compared to wild-type, overview

additional information

8 entries

K25A/E189S

site-directed mutagenesis, used as wild-type

K25A/E189S

site-directed mutagenesis, the double-site mutant show 1.8times higher enzyme activity and 2.1times higher catalytic efficiency, 1.88 and 3.32times higher inhibitory constant of alpha-ketoisovalerate and D-pantothenic acid (D-PA), respectively, compared to wild-type enzyme

L49A

site-directed mutagenesis, the mutant shows slightly decreased activity compared to wild-type enzyme

L49A

site-directed mutagenesis, the mutant shows decreased activity compared to wild-type enzyme

K25A/E189S

site-directed mutagenesis, used as wild-type

K25A/E189S

K25A/E189S

site-directed mutagenesis, used as wild-type

K25A/E189S

K25A/E189S

site-directed mutagenesis, used as wild-type

K25A/E189S

K25A/E189S

Corynebacterium glutamicum CCUG 27702

site-directed mutagenesis, used as wild-type

K25A/E189S

Corynebacterium glutamicum CCUG 27702

K25A/E189S

site-directed mutagenesis, used as wild-type

K25A/E189S

K25A/E189S

site-directed mutagenesis, used as wild-type

K25A/E189S

K25A/E189S

site-directed mutagenesis, used as wild-type

K25A/E189S

K25A/E189S

Corynebacterium glutamicum NBRC 12168

site-directed mutagenesis, used as wild-type

K25A/E189S

Corynebacterium glutamicum NBRC 12168

K25A/E189S

site-directed mutagenesis, used as wild-type

K25A/E189S

K25A/E189S

Corynebacterium glutamicum NRRL B-2784

site-directed mutagenesis, used as wild-type

K25A/E189S

Corynebacterium glutamicum NRRL B-2784

I212A

site-directed mutagenesis

I212A

site-directed mutagenesis, the mutant tolerates 3-monosubstituted 2-oxoacids with linear, branched, or cyclic substituents, mutant substrate specificity compared to wild-type, overview

I212A

site-directed mutagenesis

I212A

site-directed mutagenesis, the mutant tolerates 3-monosubstituted 2-oxoacids with linear, branched, or cyclic substituents, mutant substrate specificity compared to wild-type, overview

additional information

panB100 mutant has a deletion of G-268

additional information

panB100 mutant has a deletion of G-268

additional information

panB mutant strain UR2 is severely deficient in enzyme, a single mutation is responsible for the lack of transferase

additional information

enhancing the thermal stability and enzyme activity of ketopantoate hydroxymethyltransferase through interface modification engineering, overview. Molecular dynamics simulations

additional information

panB mutant Hfr3000 YA139 completely lacks KPHMT

additional information

construction of several plasmid-encoded panB mutants, effects on pantothenate biosynthesis, growth inhibition of pan B mutants, overview

additional information

construction of several plasmid-encoded panB mutants, effects on pantothenate biosynthesis, growth inhibition of pan B mutants, overview

additional information

panBp654 mutant with insertion of one GC base pair upstream of the transcription start site results in an optimized panBCD promoter and a 10fold increase in transcription of the pan operon, i.e. an increased expression of panB, which is sufficient to increase pantothenate biosynthesis

show all columns Go to pH Stability Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

pH STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

4.5

rapid inactivation below

5 - 10

stable

5.5

loss of proper protein folding at pH values lower than 5.5

additional information

stable and active over a broad pH-range

show all columns Go to Temperature Stability Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

53.2

melting temperature Tm of wild-type enzyme (K25A/E189S)

treatment at 55°C largely destroys enzyme in crude extract, partially purified enzyme is more heat-stabile

rapid denaturation above

additional information

melting temperatures of point mutant enzymes, overview

Go to General Stability Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

ammonium sulfate fractionation inactivates, resistant to urea denaturation

not inactivated by borohydride reduction in the presence of excess substrates

Go to Storage Stability Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

STORAGE STABILITY

ORGANISM

UNIPROT

LITERATURE

4°C, 100 mM potassium phosphate, pH 6.8, 1 mM EDTA, 0.5 mM dithiothreitol, 6 months, almost no loss of activity

Go to Purification (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

19.3fold purification of recombinant enzyme 50fold overexpressed in E. coli panB mutant Hfr3000 YA139/pCEJ01

affinity purification of recombinant PanB

purification of recombinant enzyme expressed in Escherichia coli BL21 (DE3)

purification of recombinant enzyme overexpressed in Escherichia coli BL21

recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography

strain K12, 2450fold purification

485699, 485701

Go to Cloned (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

expressed in Escherichia coli strain BW25113 or MG1655

expressed in Escherichia coli W3110 cells

gene panB, functional recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3), and in Escherichia coli strain W3110 resulting in the engineered D-PA-producing strain Escherichia coli W3110 DPA-11 containing plasmid pTrc99A-panBpanC

gene panB, phylogenetic analysis, genes panBC in Rhizobiales with multipartite genomes, overview

gene panB, recobinant expression of wild-type an dmutant enzymes in Escherichia coli strain W3110

panB gene coding for enzyme is located together with panE in the intervall purE-tre of the chromosome

panB gene encoding enzyme is cloned and overexpressed in Escherichia coli BL21 (DE3)

panB gene encoding enzyme is cloned, sequenced and 50fold overexpressed in Escherichia coli panB mutant Hfr3000 YA139 containing plasmid pCEJ01, gene is 792 bp long and encodes a protein of 264 amino acids, gene is likely to be cotranscribed with at least one other gene, panB, panC and panD genes are closely clustered at 3.1 min of the Escherichia coli K12 genetic map

panB gene encoding enzyme is cloned, sequenced and expressed in Escherichia coli as an active octameric enzyme, ORF encodes a protein of 349 amino acids, panB gene is closely linked to nimO gene on Aspergillus nidulans linkage group VII

panB gene encoding enzyme is cloned, sequenced and overexpressed in Escherichia coli BL21, ORF of 846 bp encodes a protein of 281 amino acids, N-terminal 37 amino acids are essential for enzyme function

panB gene encoding enzyme is clustered together with other pantothenate biosynthetic genes panC and panD at 3 min of the chromosome map, panBCD operon

PCR amplification of panB gene, which is identical to that of Mycobacterium bovis BCG

show all columns Go to Application Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

analysis

11 entries

pharmacology

synthesis

4 entries

analysis

fermentation of Escherichia coli strain W3110 expressing the DPA-11-CgKPHMT-mutant (M7-M18) for D-pantothenic acid evaluation, overview

analysis

fermentation of Escherichia coli strain W3110 expressing the DPA-11-CgKPHMT-mutant (M7-M18) for D-pantothenic acid evaluation, overview

analysis

fermentation of Escherichia coli strain W3110 expressing the DPA-11-CgKPHMT-mutant (M7-M18) for D-pantothenic acid evaluation, overview

analysis

fermentation of Escherichia coli strain W3110 expressing the DPA-11-CgKPHMT-mutant (M7-M18) for D-pantothenic acid evaluation, overview

analysis

fermentation of Escherichia coli strain W3110 expressing the DPA-11-CgKPHMT-mutant (M7-M18) for D-pantothenic acid evaluation, overview

analysis

fermentation of Escherichia coli strain W3110 expressing the DPA-11-CgKPHMT-mutant (M7-M18) for D-pantothenic acid evaluation, overview

analysis

fermentation of Escherichia coli strain W3110 expressing the DPA-11-CgKPHMT-mutant (M7-M18) for D-pantothenic acid evaluation, overview

analysis

Corynebacterium glutamicum CCUG 27702

fermentation of Escherichia coli strain W3110 expressing the DPA-11-CgKPHMT-mutant (M7-M18) for D-pantothenic acid evaluation, overview

analysis

Corynebacterium glutamicum NBRC 12168

fermentation of Escherichia coli strain W3110 expressing the DPA-11-CgKPHMT-mutant (M7-M18) for D-pantothenic acid evaluation, overview

analysis

Corynebacterium glutamicum NRRL B-2784

fermentation of Escherichia coli strain W3110 expressing the DPA-11-CgKPHMT-mutant (M7-M18) for D-pantothenic acid evaluation, overview

analysis

fermentation of Escherichia coli strain W3110 expressing the DPA-11-CgKPHMT-mutant (M7-M18) for D-pantothenic acid evaluation, overview

pharmacology

enzyme might be an attractive target for inhibitor design

pharmacology

enzyme could serve as target for anti-fungal drugs, since it is not present in mammals

synthesis

transformation of readily available canonical and non-canonical L-alpha-amino acids into 2-substituted 3-hydroxy-carboxylic acid derivatives. The biocatalytic cascade consists of an oxidative deamination of L-alpha-amino acids by an L-alpha-amino acid deaminase from Cosenzaea myxofaciens, rendering 2-oxoacid intermediates, with an ensuing aldol addition reaction to formaldehyde, catalyzed by metal-dependent (R)- or (S)-selective carboligases namely 2-oxo-3-deoxy-L-rhamnonate aldolase (YfaU) and ketopantoate hydroxymethyltransferase (KPHMT), respectively, furnishing 3-substituted 4-hydroxy-2-oxoacids

synthesis

biocatalytic synthesis of homochiral 2-hydroxy-4-butyrolactone derivatives by tandem aldol addition and carbonyl reduction: aldol addition reaction of 2-oxoacids to aldehydes using two aldolases from Escherichia coli, 3-methyl-2-oxobutanoate hydroxymethyltransferase (KPHMT), 2-keto-3-deoxy-L-rhamnonate aldolase (YfaU), and trans-o-hydroxybenzylidene pyruvate hydratase-aldolase from Pseudomonas putida (HBPA) and (ii) subsequent 2-oxogroup reduction of the aldol adduct by ketopantoate reductase from Escherichia coli (KPR) and a DELTA1-piperidine-2-carboxylate/DELTA1-pyrroline-2-carboxylate reductase from Pseudomonas syringae pv. tomato DSM 50315 (DpkA) with promiscuous ketoreductase activity

synthesis

synthesis

top print hide References Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

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

776976

brenda

Powers, S.G.; Snell, E.E.

Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties

J. Biol. Chem.

251

3786-3793

1976

Escherichia coli

6463

brenda

Powers, S.G.; Snell, E.E.

Purification and properties of ketopantoate hydroxymethyltransferase

Methods Enzymol.

204-209

1979

Escherichia coli

374973

brenda

485702

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

1844812

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.

342-346

2001

Mycobacterium tuberculosis variant bovis, Mycobacterium tuberculosis, 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

8096212

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

10503542

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

J. Bacteriol.

184

2827-2832

2002

Salmonella enterica

11976313

brenda

Sugantino, M.; Zheng, R.; Yu, M.; Blanchard, J.S.

Mycobacterium tuberculosis ketopantoate hydroxymethyltransferase: Tetrahydrofolate-independent hydroxymethyltransferase and enolization reactions with alpha-keto acids

Biochemistry

191-199

2003

Mycobacterium tuberculosis

12515554

brenda

659030

Schmitzberger, F.; Smith, A.G.; Abell, C.; Blundell, T.L.

Comparative analysis of the Escherichia coli ketopantoate hydroxymethyltransferase crystal structure confirms that it is a member of the (betaalpha)8 phosphoenolpyruvate/pyruvate superfamily

J. Bacteriol.

185

4163-4171

2003

Escherichia coli (P31057), Escherichia coli

12837791

brenda

660518

von Delft, F.; Inoue, T.; Saldanha, S.A.; Ottenhof, H.H.; Schmitzberger, F.; Birch, L.M.; Dhanaraj, V.; Witty, M.; Smith, A.G.; Blundell, T.L.; Abell, C.

Structure of E. coli ketopantoate hydroxymethyl transferase complexed with ketopantoate and Mg2+, solved by locating 160 selenomethionine sites

Structure

985-996

2003

Escherichia coli

12906829

brenda

673328

Pearce, M.J.; Arora, P.; Festa, R.A.; Butler-Wu, S.M.; Gokhale, R.S.; Darwin, K.H.

Identification of substrates of the Mycobacterium tuberculosis proteasome

EMBO J.

5423-5432

2006

Mycobacterium tuberculosis

17082771

brenda

Villasenor, T.; Brom, S.; Davalos, A.; Lozano, L.; Romero, D.; Los Santos, A.G.

Housekeeping genes essential for pantothenate biosynthesis are plasmid-encoded in Rhizobium etli and Rhizobium leguminosarum

BMC Microbiol.

2011

Rhizobium etli, Rhizobium etli CFN 42

21463532

brenda

Zhang, B.; Zhang, X.M.; Wang, W.; Liu, Z.Q.; Zheng, Y.G.

Metabolic engineering of Escherichia coli for D-pantothenic acid production

Food Chem.

294

267-275

2019

Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032

31126462

brenda

Thiaville, J.J.; Frelin, O.; Garcia-Salinas, C.; Harrison, K.; Hasnain, G.; Horenstein, N.A.; Diaz de la Garza, R.I.; Henry, C.S.; Hanson, A.D.; de Crecy-Lagard, V.

Experimental and metabolic modeling evidence for a folate-cleaving side-activity of ketopantoate hydroxymethyltransferase (PanB)

Front. Microbiol.

431

2016

Escherichia coli, Escherichia coli W3110

27065985

brenda

Moreno, C.J.; Hernandez, K.; Gittings, S.; Bolte, M.; Joglar, J.; Bujons, J.; Parella, T.; Clapes, P.

Biocatalytic synthesis of homochiral 2-hydroxy-4-butyrolactone derivatives by tandem aldol addition and carbonyl reduction

ACS Catal.

5348-5357

2023

Escherichia coli (P31057), Escherichia coli K12 (P31057)

37123603

brenda

Pickl, M.; Marin-Valls, R.; Joglar, J.; Bujons, J.; Clapes, P.

Chemoenzymatic production of enantiocomplementary 2-substituted 3-hydroxycarboxylic acids from L-alpha-amino acids

Adv. Synth. Catal.

363

2866-2876

2021

Escherichia coli (P31057), Escherichia coli K12 (P31057)

34276272

brenda

Cai, X.; Shi, X.; Wang, J.Y.; Hu, C.H.; Shen, J.D.; Zhang, B.; Liu, Z.Q.; Zheng, Y.G.

Enhancing the thermal stability and enzyme activity of ketopantoate hydroxymethyltransferase through interface modification engineering

J. Agric. Food Chem.

13186-13195

2024

Corynebacterium glutamicum (Q9X712), Corynebacterium glutamicum 534 (Q9X712), Corynebacterium glutamicum ATCC 13032 (Q9X712), Corynebacterium glutamicum BCRC 11384 (Q9X712), Corynebacterium glutamicum CCUG 27702 (Q9X712), Corynebacterium glutamicum DSM 20300 (Q9X712), Corynebacterium glutamicum JCM 1318 (Q9X712), Corynebacterium glutamicum LMG 3730 (Q9X712), Corynebacterium glutamicum NBRC 12168 (Q9X712), Corynebacterium glutamicum NCIMB 10025 (Q9X712), Corynebacterium glutamicum NRRL B-2784 (Q9X712)

38814711

brenda

Marin-Valls, R.; Hernandez, K.; Bolte, M.; Parella, T.; Joglar, J.; Bujons, J.; Clapes, P.

Biocatalytic construction of quaternary centers by aldol addition of 3,3-disubstituted 2-oxoacid derivatives to aldehydes

J. Am. Chem. Soc.

142

19754-19762

2020

Escherichia coli (P31057), Escherichia coli K12 (P31057)

33147013

brenda