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Information on EC 2.1.2.11 - 3-methyl-2-oxobutanoate hydroxymethyltransferase
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EC Tree
2.1.2.11 3-methyl-2-oxobutanoate hydroxymethyltransferaseSpecify your search results
Word Map
- 2.1.2.11
-
pantothen
-
auxotrophs
-
aldol
- l-valine
- beta-alanine
-
pane
-
betaalpha8
- 2-oxoacids
- pharmacology
- alpha-ketobutyrate
-
decameric
- 4'-phosphopantetheine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
ketopantoate hydroxymethyltransferase, kphmt, 3-methyl-2-oxobutanoate hydroxymethyltransferase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5,10-methylene tetrahydrofolate:alpha-ketoisovalerate hydroxymethyltransferase
-
-
-
-
alpha-ketoisovalerate hydroxymethyltransferase
-
-
-
-
dehydropantoate hydroxymethyltransferase
-
-
-
-
hydroxymethyltransferase, ketopantoate
-
-
-
-
ketopantoate hydroxymethyltransferase
KHMT
-
-
-
-
KPHMT
MOHMT
oxopantoate hydroxymethyltransferase
-
-
-
-
PanB
ketopantoate hydroxymethyltransferase
-
-
-
-
KPHMT
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate
stereochemistry
-
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate
stereochemistry
-
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate
class II aldolase
-
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate
sequential kinetic mechanism, chemical mechanism
-
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydroxymethyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
5,10-methylenetetrahydrofolate:3-methyl-2-oxobutanoate hydroxymethyltransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
56093-17-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,10-methylenetetrahydrofolate + 2-oxo-4-methylthiobutyrate
tetrahydrofolate + ?
-
about 50% of the activity with 3-methyl-2-oxobutanoate
-
-
?
5,10-methylenetetrahydrofolate + 2-oxobutyrate
tetrahydrofolate + ?
-
about 50% of the activity with 3-methyl-2-oxobutanoate
-
-
?
5,10-methylenetetrahydrofolate + 2-oxopentanoate
tetrahydrofolate + ?
-
about 30% of the activity with 3-methyl-2-oxobutanoate
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
5,10-methylenetetrahydrofolate + 3-methyl-2-oxopentanoate
?
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxopentanoate
tetrahydrofolate + ?
-
about 65% of the activity with 3-methyl-2-oxobutanoate
-
-
?
5,10-methylenetetrahydrofolate + pyruvate
tetrahydrofolate + ?
-
about 20% of the activity with 3-methyl-2-oxobutanoate
-
-
?
formaldehyde + 3-methyl-2-oxobutanoate
2-dehydropantoate
-
enzyme catalyzes methylenetetrahydrofolate-independent hydroxymethyltransferase reaction between free formaldehyde and alpha-ketoisovalerate, formaldehyde is unlikely to be the natural substrate
-
?
tetrahydropteroyldiglutamate + 2-dehydropantoate
5,10-methylenetetrahydropteroyldiglutamate + 3-methyl-2-oxobutanoate + H2O
-
-
-
-
r
tetrahydropteroylheptaglutamate + 2-dehydropantoate
5,10-methylenetetrahydropteroylheptaglutamate + 3-methyl-2-oxobutanoate + H2O
-
-
-
-
r
tetrahydropteroylhexaglutamate + 2-dehydropantoate
5,10-methylenetetrahydropteroylhexaglutamate + 3-methyl-2-oxobutanoate + H2O
-
-
-
-
r
tetrahydropteroylpentaglutamate + 2-dehydropantoate
5,10-methylenetetrahydropteroylpentaglutamate + 3-methyl-2-oxobutanoate + H2O
-
-
-
-
r
tetrahydropteroyltetraglutamate + 2-dehydropantoate
5,10-methylenetetrahydropteroyltetraglutamate + 3-methyl-2-oxobutanoate + H2O
-
-
-
-
r
tetrahydropteroyltriglutamate + 2-dehydropantoate
5,10-methylenetetrahydropteroyltriglutamate + 3-methyl-2-oxobutanoate + H2O
-
-
-
-
r
5,10-methylenetetrahydrofolate + 2-oxobutyrate
?
-
also a good substrate
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
essential for the biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of pantothenate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
-
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
formation of ketopantoate, syn. 2-keto-3,3-dimethyl-4-hydroxybutyrate, tetrahydrofolate-dependent enzyme
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
synthesis of ketopantoate, the following components can replace tetrahydrofolate: tetrahydropteroylmono-, di-, tri-, tetra-, penta-, hexa-, and heptaglutamate, absolute requirement for tetrahydrofolate, only the L-isomer is active
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
forms 2-oxopantoate, syn. 3-hydroxymethyl-3-methyl-2-oxobutanoic acid, from 2-oxoisovalerate with retention of configuration at C-3
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
condensation of alpha-ketoisovalerate with the C-1 donor takes place stereospecifically at C-3 and proceeds in a retention mode at C-3, 5,10-methylenetetrahydrofolate-dependent enzyme
-
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
specificity for alpha-ketoisovalerate is less rigid than for tetrahydrofolate
synthesis of ketopantoate, the following components can replace tetrahydrofolate: tetrahydropteroylmono-, di-, tri-, tetra-, penta-, hexa-, and heptaglutamate, absolute requirement for tetrahydrofolate, only the L-isomer is active
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
inversion of the configuration at C-3 of 2-ketoisovalerate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
enzyme is responsible for catalysis of ketopantoate formation in vivo
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
catalytic activity is regulated by the products of the reaction path of which it is one component
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first step in pantoate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
enzyme may be the rate-limiting reaction in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of pantothenate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
enzyme may be the rate-limiting reaction in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
-
-
r
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
-
-
-
-
?
additional information
?
-
-
no substrates: pyruvate, isovalerate, D- and L-valine, 3-methyl-2-butanone
-
-
?
additional information
?
-
-
enzyme catalyzes deuterium exchange in the methylenetetrahydrofolate-independent enolization of alpha-ketoisovalerate or other alpha-keto acids with decreasing efficiency: alpha-ketoisovalerate, alpha-ketobutyrate, alpha-ketovalerate, pyruvate, alpha-ketomethylthiobutyrate, alpha-ketoisocaproate, stereochemistry, first step in the reaction leading to ketopantoate is the enolization of alpha-ketoisovalerate to form the stabilized carbanion
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
essential for the biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of pantothenate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
enzyme is responsible for catalysis of ketopantoate formation in vivo
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
catalytic activity is regulated by the products of the reaction path of which it is one component
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of coenzyme A
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first step in pantoate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
enzyme may be the rate-limiting reaction in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
biosynthesis of pantothenate
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
enzyme may be the rate-limiting reaction in pantothenate biosynthesis
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate
tetrahydrofolate + 2-dehydropantoate
-
first committed step in pantothenate biosynthesis
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
-
-
-
-
?
5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O
tetrahydrofolate + 2-dehydropantoate
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no requirement of pyridoxal 5-phosphate as cofactor
-
5,10-methylenetetrahydrofolate
-
5,10-methylenetetrahydrofolate as cofactor
5,10-methylenetetrahydrofolate
-
5,10-methylenetetrahydrofolate-dependent enzyme
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
Ni2+
Zn2+
additional information
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+
-
substrate enolization is divalent metal-dependent with a preference for metal ions in decreasing order: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Co2+
-
Km: 0.33 mM, the reaction is divalent metal-dependent with descending order of preference: Mg2+, Zn2+, Co2+, Ni2+, Ca2+
Mg2+
-
activates and is required for activity, 0.1 mM Mg2+ is most active, Mn2+, Ni2+, Co2+ and Zn2+ are progressively less active, restores activity after dialysis
Mg2+
-
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+
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+
-
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
-
metalloenzyme, inactive in absence of divalent metals, enzyme binds metal ions that assist in the polarization of the carbonyl group and stabilize the enolate anion
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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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.
Tuberculosis
Mycobacterium tuberculosis ketopantoate hydroxymethyltransferase: tetrahydrofolate-independent hydroxymethyltransferase and enolization reactions with alpha-keto acids.
Tuberculosis
The crystal structure of the first enzyme in the pantothenate biosynthetic pathway, ketopantoate hydroxymethyltransferase, from M tuberculosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.9
formaldehyde
-
methylenetetrahydrofolate: formaldehyde + tetrahydrofolate
0.18
tetrahydrofolate
-
forward and reverse reaction, methylenetetrahydrofolate: formaldehyde + tetrahydrofolate
additional information
additional information
-
low Km-values for its substrates
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 7.5
additional information
7 - 7.5
-
rate of substrate enolization is pH-dependent with optimal activity in the range of
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
