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

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
2.1.2.11
-
RECOMMENDED NAME
GeneOntology No.
3-methyl-2-oxobutanoate hydroxymethyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
class II aldolase
-
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
stereochemistry
-
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
class II aldolase; stereochemistry
-
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
sequential kinetic mechanism, chemical mechanism; stereochemistry
-
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
class II aldolase
Escherichia coli K12
-
-
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydroxymethyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Metabolic pathways
-
Pantothenate and CoA biosynthesis
-
phosphopantothenate biosynthesis I
-
phosphopantothenate biosynthesis III
-
SYSTEMATIC NAME
IUBMB Comments
5,10-methylenetetrahydrofolate:3-methyl-2-oxobutanoate hydroxymethyltransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5,10-methylene tetrahydrofolate:alpha-ketoisovalerate hydroxymethyltransferase
-
-
-
-
alpha-ketoisovalerate hydroxymethyltransferase
-
-
-
-
dehydropantoate hydroxymethyltransferase
-
-
-
-
hydroxymethyltransferase, ketopantoate
-
-
-
-
ketopantoate hydroxymethyl transferase
-
-
ketopantoate hydroxymethyltransferase
-
-
-
-
ketopantoate hydroxymethyltransferase
-
-
ketopantoate hydroxymethyltransferase
-
-
ketopantoate hydroxymethyltransferase
-
-
ketopantoate hydroxymethyltransferase
Rhizobium etli CFN42
-
-
-
KHMT
-
-
-
-
KPHMT
-
-
-
-
KPHMT
Rhizobium etli CFN42
-
-
-
MOHMT
Rhizobium etli CFN42
-
-
-
oxopantoate hydroxymethyltransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
56093-17-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strains 168, BD170, UR1, UR4
-
-
Manually annotated by BRENDA team
wild-type strains biA1 and yA2, strain G1765
Uniprot
Manually annotated by BRENDA team
strain ATCC 23783
-
-
Manually annotated by BRENDA team
strain K12; strains W and B
-
-
Manually annotated by BRENDA team
Escherichia coli K12
strain K12
-
-
Manually annotated by BRENDA team
BCG, strain 1173-P2, live vaccine against tuberculosis, used for superficial bladder cancer immunotherapy
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
strain KIT 10468
-
-
Manually annotated by BRENDA team
Mycobacterium tuberculosis KIT 10468
strain KIT 10468
-
-
Manually annotated by BRENDA team
genomic gene panB, and a second putative MOHMT enzyme, RHE_PE00443, similar to the product of panB, is encoded on plasmid p42e
-
-
Manually annotated by BRENDA team
Rhizobium etli CFN42
genomic gene panB, and a second putative MOHMT enzyme, RHE_PE00443, similar to the product of panB, is encoded on plasmid p42e
-
-
Manually annotated by BRENDA team
serovar typhimurium
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
Rhizobium etli CFN42
-
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
Rhizobium etli CFN42
-
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
-
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
Rhizobium etli CFN42
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5,10-methylenetetrahydrofolate + 2-oxo-4-methylthiobutyrate
tetrahydrofolate + ?
show the reaction diagram
-
about 50% of the activity with 3-methyl-2-oxobutanoate
-
-
?
5,10-methylenetetrahydrofolate + 2-oxobutyrate
?
show the reaction diagram
-
-
-
-
?
5,10-methylenetetrahydrofolate + 2-oxobutyrate
?
show the reaction diagram
-
also a good substrate
-
-
?
5,10-methylenetetrahydrofolate + 2-oxobutyrate
?
show the reaction diagram
Escherichia coli K12
-
-
-
-
?
5,10-methylenetetrahydrofolate + 2-oxobutyrate
tetrahydrofolate + ?
show the reaction diagram
-
about 50% of the activity with 3-methyl-2-oxobutanoate
-
-
?
5,10-methylenetetrahydrofolate + 2-oxopentanoate
?
show the reaction diagram
-
-
-
-
?
5,10-methylenetetrahydrofolate + 2-oxopentanoate
?
show the reaction diagram
Escherichia coli K12
-
-
-
-
?
5,10-methylenetetrahydrofolate + 2-oxopentanoate
tetrahydrofolate + ?
show the reaction diagram
-
about 30% of the activity with 3-methyl-2-oxobutanoate
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
-
-
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
-
-
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-, Q9Y7B6
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
inversion of the configuration at C-3 of 2-ketoisovalerate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-, Q9Y7B6
essential for the biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
first step in pantoate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
biosynthesis of pantothenate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
biosynthesis of pantothenate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
enzyme may be the rate-limiting reaction in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
enzyme may be the rate-limiting reaction in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
Mycobacterium tuberculosis KIT 10468
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
Mycobacterium tuberculosis KIT 10468
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
Escherichia coli K12
-
-
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
show the reaction diagram
Escherichia coli K12
-
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
show the reaction diagram
Escherichia coli K12
-
-
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
show the reaction diagram
Escherichia coli K12
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
Escherichia coli K12
-
-
-
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
Escherichia coli K12
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxopentanoate
?
show the reaction diagram
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxopentanoate
?
show the reaction diagram
Escherichia coli K12
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxopentanoate
tetrahydrofolate + ?
show the reaction diagram
-
about 65% of the activity with 3-methyl-2-oxobutanoate
-
-
?
5,10-methylenetetrahydrofolate + pyruvate
tetrahydrofolate + ?
show the reaction diagram
-
about 20% of the activity with 3-methyl-2-oxobutanoate
-
-
?
formaldehyde + 3-methyl-2-oxobutanoate
2-dehydropantoate
show the reaction diagram
-
enzyme catalyzes methylenetetrahydrofolate-independent hydroxymethyltransferase reaction between free formaldehyde and alpha-ketoisovalerate, formaldehyde is unlikely to be the natural substrate
-
?
formaldehyde + tetrahydrofolate
methylentetrahydrofolate
show the reaction diagram
-
-
-
-
-
formaldehyde + tetrahydrofolate
methylentetrahydrofolate
show the reaction diagram
-
-
-
?
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
-
-
-
additional information
?
-
-
no substrates: pyruvate, isovalerate, D- and L-valine, 3-methyl-2-butanone
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-, Q9Y7B6
essential for the biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
first step in pantoate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
biosynthesis of pantothenate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
biosynthesis of pantothenate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
enzyme may be the rate-limiting reaction in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
-
enzyme may be the rate-limiting reaction in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
Mycobacterium tuberculosis KIT 10468
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
Escherichia coli K12
-
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
show the reaction diagram
Escherichia coli K12
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
show the reaction diagram
Escherichia coli K12
-
first committed step in pantothenate biosynthesis
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5,10-methylenetetrahydrofolate
-
5,10-methylenetetrahydrofolate-dependent enzyme
5,10-methylenetetrahydrofolate
-
-
5,10-methylenetetrahydrofolate
-
-
5,10-methylenetetrahydrofolate
-
-
5,10-methylenetetrahydrofolate
-, Q9Y7B6
-
5,10-methylenetetrahydrofolate
-
-
tetrahydrofolate
-
tetrahydrofolate-dependent reaction
tetrahydrofolate
-
absolute requirement for tetrahydrofolate
tetrahydrofolate
-
requires tetrahydrofolate
tetrahydrofolate
-
-
tetrahydrofolate
-
-
tetrahydrofolate
-, Q9Y7B6
-
tetrahydrofolate
-
-
5,10-methylenetetrahydrofolate
-
5,10-methylenetetrahydrofolate as cofactor
additional information
-
no requirement of pyridoxal 5-phosphate as cofactor
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
Km: 0.27 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+; substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: 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+
-
Km: 0.33 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+; substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: 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+
-
Km: 0.61 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+; substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
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+
-
Km: 0.45 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+; substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: 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+
-
Km: 0.08 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+; substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Mn2+
-
requires Mg2+, Mn2+, Co2+ and Zn2+ are progressively less active
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
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-Methyl-2-butanone
-
5 mM, 27% inhibition
coenzyme A
-
above 1 mM
D-valine
-
5 mM, 16% inhibition
formaldehyde
-
0.8 mM, partial inhibition
formaldehyde
-
0.8 mM, partial inhibition; forward reaction
Isovalerate
-
5 mM, 39% inhibition
Pantoate
-
0.05 mM or above
pantothenate
-
0.5 mM or above
pyruvate
-
5 mM, 38% inhibition
tetrahydrofolate
-
0.38 mM, partial inhibition
tetrahydrofolate
-
0.38 mM, partial inhibition; forward reaction
L-valine
-
5 mM, 23% inhibition
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.9
-
2-oxobutyrate
-
-
25
-
2-Oxopentanoate
-
-
0.24
-
3-methyl-2-oxobutanoate
-
-
1.1
-
3-methyl-2-oxobutanoate
-
-
5.9
-
3-methyl-2-oxopentanoate
-
-
0.82
-
5,10-methylenetetrahydrofolate
-
-
5.9
-
formaldehyde
-
methylenetetrahydrofolate: formaldehyde + tetrahydrofolate
5.9
-
formaldehyde
-
-
0.15
-
ketopantoate
-
-
0.18
-
tetrahydrofolate
-
forward and reverse reaction, methylenetetrahydrofolate: formaldehyde + tetrahydrofolate
0.18
-
tetrahydrofolate
-
-
0.25
-
tetrahydropteroyldiglutamate
-
-
0.29
-
tetrahydropteroylheptaglutamate
-
-
0.17
-
tetrahydropteroylhexaglutamate
-
-
0.33
-
tetrahydropteroylmonoglutamate
-
-
0.1
-
Tetrahydropteroylpentaglutamate
-
-
0.1
-
tetrahydropteroyltetraglutamate
-
-
0.18
-
Tetrahydropteroyltriglutamate
-
-
0.16
-
ketopantoate
-
-
additional information
-
additional information
-
low Km-values for its substrates
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.78
-
3-methyl-2-oxobutanoate
-
-
0.783
-
3-methyl-2-oxobutanoate
-
-
0.78
-
5,10-methylenetetrahydrofolate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
-, Q9Y7B6
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
-
-
purified recombinant enzyme from strain Hfr3000 YA139/pCEJ01
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
7.5
-
; rate of substrate enolization is pH-dependent with optimal activity in the range of
8
-
-
at or below
additional information
-
-
pI: 4.4
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
9
-
about 50% of activity maximum at pH 6 and 9, inactive below pH 5
10
-
-
no ketopantoate formation above pH 10
additional information
-
-
stable and active over a broad pH-range
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
37
-
-, Q9Y7B6
assay at
70
80
-
reverse reaction, activity decreases rapidly above 80C
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
most of recombinant enzyme is found in a soluble fraction
-
Manually annotated by BRENDA team
Mycobacterium tuberculosis KIT 10468
-
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Burkholderia pseudomallei (strain 1710b)
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Escherichia coli (strain K12)
Neisseria meningitidis serogroup B (strain MC58)
Neisseria meningitidis serogroup B (strain MC58)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
120000
-
-
gel filtration
174000
-
-
recombinant enzyme, gel filtration
255000
-
-
sedimentation equilibrium
285000
-
-
gel filtration
340000
-
-, Q9Y7B6
recombinant enzyme expressed in Escherichia coli, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 29337, calculated from the amino acid sequence, x * 35000, recombinant enzyme expressed in Escherichia coli BL21, SDS-PAGE
decamer
-
10 * 27000, SDS-PAGE, 10 * 25700, amino acid analysis
decamer
Escherichia coli K12
-
10 * 27000, SDS-PAGE, 10 * 25700, amino acid analysis
-
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
-, Q9Y7B6
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
hexamer
Escherichia coli K12
-
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
-
additional information
-
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
no modification
-
-
no modification
Escherichia coli K12
-
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
comparative analysis of the Escherichia coli ketopantoate hydroxymethyltransferase crystal structure confirms that it is a member of the (betaalpha)8 phosphoenolpyruvate/pyruvate superfamily
P31057
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+
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
55
-
-
treatment at 55C largely destroys enzyme in crude extract, partially purified enzyme is more heat-stabile
80
-
-
rapid denaturation above
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate fractionation inactivates, resistant to urea denaturation
-
not inactivated by borohydride reduction in the presence of excess substrates
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 100 mM potassium phosphate, pH 6.8, 1 mM EDTA, 0.5 mM dithiothreitol, 6 months, almost no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
affinity purification of recombinant PanB
-, Q9Y7B6
19.3fold purification of recombinant enzyme 50fold overexpressed in E. coli panB mutant Hfr3000 YA139/pCEJ01
-
strain K12, 2450fold purification
-
purification of recombinant enzyme overexpressed in Escherichia coli BL21
-
purification of recombinant enzyme expressed in Escherichia coli BL21 (DE3)
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
panB gene coding for enzyme is located together with panE in the intervall purE-tre of the chromosome
-
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
-, Q9Y7B6
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 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 cloned and overexpressed in Escherichia coli BL21 (DE3)
-
PCR amplification of panB gene, which is identical to that of Mycobacterium bovis BCG
-
gene panB, phylogenetic analysis, genes panBC in Rhizobiales with multipartite genomes, overview
-
panB gene encoding enzyme is clustered together with other pantothenate biosynthetic genes panC and panD at 3 min of the chromosome map, panBCD operon
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
panB mutant strain UR2 is severely deficient in enzyme, a single mutation is responsible for the lack of transferase
additional information
-, Q9Y7B6
panB100 mutant has a deletion of G-268
additional information
-
panB mutant Hfr3000 YA139 completely lacks KPHMT
additional information
Escherichia coli K12
-
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
Rhizobium etli CFN42
-
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pharmacology
-, Q9Y7B6
enzyme could serve as target for anti-fungal drugs, since it is not present in mammals
pharmacology
-
enzyme might be an attractive target for inhibitor design