Information on EC 1.2.7.7 - 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)

Word Map on EC 1.2.7.7
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
1.2.7.7
-
RECOMMENDED NAME
GeneOntology No.
3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO2 + 2 reduced ferredoxin + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidative decarboxylation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
Valine, leucine and isoleucine degradation
-
-
isoleucine metabolism
-
-
leucine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
3-methyl-2-oxobutanoate:ferredoxin oxidoreductase (decarboxylating; CoA-2-methylpropanoylating)
The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo-pentanoate, 2-oxobutyrate and 3-methylthiopropanamine. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.1, pyruvate synthase, and EC 1.2.7.3, 2-oxoglutarate synthase.
CAS REGISTRY NUMBER
COMMENTARY hide
60320-97-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain DSM 2133
-
-
Manually annotated by BRENDA team
ES-4
-
-
Manually annotated by BRENDA team
ES-4
-
-
Manually annotated by BRENDA team
ES-1
-
-
Manually annotated by BRENDA team
ES-1
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-keto-3-methylvalerate + CoA + oxidized ferredoxin
2-methylbutanoyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
2-ketobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
2-ketocaproate + CoA + oxidized ferredoxin
pentanoyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
2-ketoisocaproate + CoA + oxidized ferredoxin
S-(3-methylbutanoyl)-CoA + CO2 + reduced ferredoxin
show the reaction diagram
2-ketoisohexanoate + CoA + benzyl viologen
isopentanoyl-CoA + CO2 + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
2-ketoisovalerate + CoA + benzyl viologen
S-(2-methylpropanoyl)-CoA + CO2 + reduced benzyl viologen
show the reaction diagram
2-ketoisovalerate + CoA + oxidized ferredoxin
?
show the reaction diagram
-
-
-
-
?
2-ketoisovalerate + CoA + oxidized ferredoxin
S-(2-methylpropanoyl)-CoA + CO2 + reduced ferredoxin
show the reaction diagram
2-ketovalerate + CoA + benzyl viologen
butanoyl-CoA + CO2 + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
3-methyl-2-oxobutanoate + CoA + oxidized ferredoxin
S-(2-methylpropanoyl)-CoA + CO2 + reduced ferredoxin
show the reaction diagram
-
-
-
-
?
4-methylthio-2-oxobutanoate + CoA + oxidized ferredoxin
3-methylthio-2-oxopropanoyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
glyoxylate + CoA + oxidized ferredoxin
formyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
hydroxyphenylpyruvate + CoA + oxidized ferredoxin
4-hydroxyphenylacetyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
indolpyruvate + CoA + oxidized ferredoxin
indolacetyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
isobutyryl-CoA + CO2 + reduced benzyl viologen
2-oxoisopentanoate + CoA + benzyl viologen
show the reaction diagram
phenylglyoxylate + CoA + oxidized ferredoxin
benzoyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
phenylpyruvate + CoA + oxidized ferredoxin
phenylacetyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
pyruvate + CoA + oxidized ferredoxin
acetyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-methyl-2-oxobutanoate + CoA + oxidized ferredoxin
S-(2-methylpropanoyl)-CoA + CO2 + reduced ferredoxin
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4Fe-4S cluster
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
80C, complete loss of activity
iodoacetate
-
23C, in a concentration-dependent manner
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012 - 0.15
2-keto-3-methylvalerate
0.17 - 0.38
2-Ketobutyrate
0.049 - 0.311
2-ketocaproate
0.026 - 0.176
2-ketoisocaproate
0.094 - 1.3
2-ketoisovalerate
0.276
2-ketomethylisobutyrate
-
pH 6.9, 85C, under argon
0.058
4-methylthio-2-oxobutanoate
-
pH 6.9, 85C, under argon
0.048
CO2
-
pH 7.0, 85C, under argon
0.004 - 0.05
CoA
0.021
coenzyme A
-
-
0.017
Ferredoxin
-
pH 6.9, 85C, under argon
-
0.25
isobutyryl-CoA
-
pH 7.0, 85C, under argon
0.6
phenylglyoxalate
-
pH 6.9, 85C, under argon
0.466
phenylglyoxylate
-
pH 6.9, 85C, under argon
0.22
phenylpyruvate
-
pH 6.9, 85C, under argon
0.75 - 2.8
pyruvate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.27 - 2.07
2-keto-3-methylvalerate
1.47 - 22.3
2-Ketobutyrate
0.933 - 1
2-ketocaproate
2 - 2.47
2-ketoisocaproate
3 - 3.67
2-ketoisovalerate
1.07
2-ketomethylisobutyrate
Pyrococcus sp.
-
pH 6.9, 85C, under argon
0.667
4-methylthio-2-oxobutanoate
Thermococcus litoralis
-
pH 6.9, 85C, under argon
5 - 5.6
CoA
1.53
Ferredoxin
Thermococcus litoralis
-
pH 6.9, 85C, under argon
-
0.0133
glyoxylate
Thermococcus litoralis
-
pH 6.9, 85C, under argon
0.833
hydroxyphenylpyruvate
Thermococcus litoralis
-
pH 6.9, 85C, under argon
0.433
indolpyruvate
Thermococcus litoralis
-
pH 6.9, 85C, under argon
0.833
phenylglyoxalate
Thermococcus litoralis
-
pH 6.9, 85C, under argon
1.33
phenylglyoxylate
Pyrococcus sp.
-
pH 6.9, 85C, under argon
0.467 - 0.6
phenylpyruvate
0.267 - 1.73
pyruvate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.76
-
cell-free extract
3.8
-
Hydroxyapatite purified
4.3
-
Q Sepharose purified
128
-
Red TOYOPEARL purified
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.4
-
activity assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
-
activity assay, VOR activity is routinely assayed by means of CoA-dependent reduction of methyl viologen with 2-ketoisovalerate at 80C
90
-
ketoisovalerate oxidation
93
-
the optimal temperature for the 2-ketoisovalerate methyl viologen oxidoreductase assay is determined to be 93C
98
-
ketoisovalerate oxidation
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11851
-
alpha,beta,gamma,delta, x * 43960 + x * 34766 + x * 20033 + x * 11851, SDS PAGE, amino acid sequences
15000
-
x * 55000 + x * 37000 + x * 15000, SDS-PAGE
20033
-
alpha,beta,gamma,delta, x * 43960 + x * 34766 + x * 20033 + x * 11851, SDS PAGE, amino acid sequences
22000
-
gamma subunit, determined by SDS-PAGE
31000
-
beta subunit, determined by SDS-PAGE
34766
-
alpha,beta,gamma,delta, x * 43960 + x * 34766 + x * 20033 + x * 11851, SDS PAGE, amino acid sequences
37000
-
x * 55000 + x * 37000 + x * 15000, SDS-PAGE
43960
-
alpha,beta,gamma,delta, x * 43960 + x * 34766 + x * 20033 + x * 11851, SDS PAGE, amino acid sequences
45000
-
alpha subunit, determined by SDS-PAGE
55000
-
x * 55000 + x * 37000 + x * 15000, SDS-PAGE
218000
-
native enzyme, determined by gel filtration
220000
-
native enzyme, determined by analytical centrifugation
230000
-
calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
pH 6.0: less than 50% loss of activity, pH 8.0: 25% loss of activity
644696
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85
-
pH 8.0, Tris-HCl, half-life 3 h
95
-
pH 8.0, Tris-HCl, half-life 50 min
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
about 50% of the enzyme activity in the cell extract is lost after exposure to air for 2 min, no activity loss if the extract is under argon
-
644696
enzyme is irreversibly inactivated by oxygen
-
639362
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cell-free extracts are loaded onto a Q Sepharose Fast Flow column, activity containing fractions are loaded onto a hydroxyapatite column, finally a TOYOPEARL column is used
-
under anaerobic conditions
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
Show AA Sequence (666 entries)
Please use the Sequence Search for a specific query.