Information on EC 4.1.1.72 - branched-chain-2-oxoacid decarboxylase

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

EC NUMBER
COMMENTARY hide
4.1.1.72
-
RECOMMENDED NAME
GeneOntology No.
branched-chain-2-oxoacid decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(3S)-3-methyl-2-oxopentanoate = 2-methylbutanal + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
butanol and isobutanol biosynthesis (engineered)
-
-
L-isoleucine degradation II
-
-
L-valine degradation II
-
-
methionine metabolism
-
-
pyruvate fermentation to isobutanol (engineered)
-
-
SYSTEMATIC NAME
IUBMB Comments
(3S)-3-methyl-2-oxopentanoate carboxy-lyase (2-methylbutanal-forming)
Acts on a number of 2-oxo acids, with a high affinity towards branched-chain substrates. The aldehyde formed may be enzyme-bound, and may be an intermediate in the bacterial system for the biosynthesis of branched-chain fatty acids.
CAS REGISTRY NUMBER
COMMENTARY hide
63653-19-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(indol-3-yl)pyruvate
(indol-3-yl)acetaldehyde + CO2
show the reaction diagram
2-oxo-3-methylpentanoate
2-methylbutanal + CO2
show the reaction diagram
-
-
-
?
2-oxo-3-methylvalerate
2-methylbutanal + CO2
show the reaction diagram
-
the enzymatic activity toward 2-oxo-3-methylvalerate is 1.5times higher than the activity toward 2-oxo-isovalerate
-
-
?
2-oxo-3-phenylpropanoic acid
phenylacetaldehyde + CO2
show the reaction diagram
-
at 30 mM 8.6% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
2-oxobutanoic acid
propanal + CO2
show the reaction diagram
2-oxobutyrate
propionaldehyde + CO2
show the reaction diagram
-
-
-
?
2-oxoglutarate
CO2 + succinate semialdehyde
show the reaction diagram
-
5% of the activity with L-3-methyl-2-oxopentanoate
-
-
-
2-oxohexanoate
n-pentanal + CO2
show the reaction diagram
-
-
-
?
2-oxohexanoic acid
pentanal + CO2
show the reaction diagram
2-oxoisohexanoate
? + CO2
show the reaction diagram
-
-
-
?
2-oxoisohexanoate
CO2 + isopentanal
show the reaction diagram
2-oxoisopentanoate
2-methylpropanal + CO2
show the reaction diagram
-
-
-
?
2-oxoisopentanoate
CO2 + isobutanal
show the reaction diagram
-
63% of the activity with L-3-methyl-
-
-
?
2-oxoisovalerate
2-methylpropanal + CO2
show the reaction diagram
-
-
-
-
?
2-oxopentanoate
n-butanal + CO2
show the reaction diagram
-
-
-
?
2-oxopentanoic acid
butanal + CO2
show the reaction diagram
2-oxopropanoic acid
acetaldehyde + CO2
show the reaction diagram
-
at 30 mM 1.2% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
3-(4-hydroxyphenyl)-2-oxopropanoic acid
(4-hydroxyphenyl)-acetaldehyde + CO2
show the reaction diagram
-
at 30 mM 6% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
3-methyl-2-oxobutanoic acid
2-methylpropanal + CO2
show the reaction diagram
3-methyl-2-oxobutyrate
3-methylpropanal + CO2
show the reaction diagram
3-methyl-2-oxopentanoate
3-methylbutanal + CO2
show the reaction diagram
3-methyl-2-oxopentanoate
CO2 + 2-methylbutanal
show the reaction diagram
3-methyl-2-oxopentanoic acid
2-methylbutanal + CO2
show the reaction diagram
4-(4-hydroxyphenyl)-2-oxobutanoic acid
3-(4-hydroxyphenyl)-propanal + CO2
show the reaction diagram
-
at 30 mM 1.6% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
4-(methylsulfanyl)-2-oxobutanoic acid
3-(methylsulfanyl)-propanal + CO2
show the reaction diagram
-
at 30 mM 18% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
4-hydroxyphenylpyruvate
4-hydroxyphenylacetaldehyde + CO2
show the reaction diagram
4-methyl-2-oxohexanoic acid
3-methylpentanal + CO2
show the reaction diagram
-
at 30 mM 19% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
4-methyl-2-oxopentanoate
4-methylbutanal + CO2
show the reaction diagram
4-methyl-2-oxopentanoic acid
3-methylbutanal + CO2
show the reaction diagram
4-methylthio-2-oxobutanoic acid
3-methylthiopropanal + CO2
show the reaction diagram
10% of the rate with 3-methyl-2-oxobutanoic acid
-
-
?
5-(4-hydroxyphenyl)-2-oxopentanoic acid
4-(4-hydroxyphenyl)-butanal + CO2
show the reaction diagram
-
at 30 mM 1.1% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
alpha-isocaproic acid
3-methylbutanal + CO2
show the reaction diagram
-
-
-
?
benzaldehyde + CO2
(R)-benzoin
show the reaction diagram
-
self-carboligation
-
-
?
benzoylformate
? + CO2
show the reaction diagram
-
-
-
?
indole-3-pyruvate
?
show the reaction diagram
-
at 1 mM 0.85% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
isovaleraldehyde
?
show the reaction diagram
-
self-carboligation
-
-
?
L-3-methyl-2-oxopentanoate
CO2 + 2-methylbutanal
show the reaction diagram
oxo(phenyl)acetic acid
benzaldehyde + CO2
show the reaction diagram
-
at 30 mM 8.4% activity relative to 3-methyl-2-oxobutanoic acid
-
-
?
Phenylpyruvate
Phenylacetaldehyde + CO2
show the reaction diagram
Pyruvate
Acetaldehyde + CO2
show the reaction diagram
pyruvate
CO2 + ethanal
show the reaction diagram
-
25% of the activity with L-3-methyl-2-oxopentanoate
-
-
-
pyruvate
ethanal + CO2
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-oxopentanoate
CO2 + 2-methylbutanal
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ferricyanide
-
stimulates
Mg2+
-
dependent
additional information
-
no requirement for MgCl2
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-[(R)-1-hydroxyethyl]deaza thiamine diphosphate
-
0.1 mM
pyruvate
weak substrate inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NaCl
20% increase in activity at 1 M
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09
(indol-3-yl)pyruvate
-
20.25
2-oxo-3-methylpentanoate
-
0.127
2-oxo-3-phenylpropanoate
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
138.3
2-oxobutyrate
-
0.83
2-Oxohexanoate
-
0.6
2-oxohexanoic acid
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
2
2-Oxoisohexanoate
-
25C, pH 7.2
0.05 - 0.39
2-oxoisovalerate
1.21
2-Oxopentanoate
-
1.3
2-Oxopentanoic acid
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
29.77
2-Oxopropanoic acid
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
0.63
3-(4-hydroxyphenyl)-2-oxopropanoic acid
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
5.02
3-methyl-2-oxobutanoic acid
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
0.87
3-methyl-2-oxopentanoate
-
25C, pH 7.2
1.3
4-(methylsulfanyl)-2-oxobutanoic acid
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
0.264
4-methyl-2-oxopentanoic acid
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
26.11
benzoylformate
-
0.234
Indole-3-pyruvate
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
0.001
L-3-Methyl-2-oxopentanoate
-
and 2-oxoisopentanoate, 2-oxoisohexanoate, value below, 30C, pH 7.5
7.5
oxo(phenyl)acetic acid
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
1.17
phenylpyruvate
-
0.00063 - 0.04
thiamine diphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.98
(indol-3-yl)pyruvate
Mycobacterium tuberculosis
P9WG37
-
19.75
2-oxo-3-methylpentanoate
Mycobacterium tuberculosis
P9WG37
-
5.98
2-oxobutyrate
Mycobacterium tuberculosis
P9WG37
-
7.06
2-Oxohexanoate
Mycobacterium tuberculosis
P9WG37
-
31.5
2-Oxoisohexanoate
Mycobacterium tuberculosis
P9WG37
-
28.35
2-oxoisopentanoate
Mycobacterium tuberculosis
P9WG37
-
0.19 - 0.57
2-oxoisovalerate
6.95
2-Oxopentanoate
Mycobacterium tuberculosis
P9WG37
-
29 - 33
3-methyl-2-oxobutyrate
23 - 27
3-methyl-2-oxopentanoate
3.89
4-hydroxyphenylpyruvate
Mycobacterium tuberculosis
P9WG37
-
7 - 8.5
4-methyl-2-oxopentanoate
18.57
benzoylformate
Mycobacterium tuberculosis
P9WG37
-
1.7 - 7.5
phenylpyruvate
2.14
pyruvate
Mycobacterium tuberculosis
P9WG37
-
0.19 - 0.53
thiamine diphosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
124
pyruvate
weak substrate inhibition is detected for pyruvate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.02
-
30C, pH 7.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
pH 6: about 60% of maximum activity, pH 9: about 55% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
BCKDC proteins in the metabolon are found in all tissues except skeletal muscle, which harbors only the five subunits
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
59780
calculated from the deduced amino acid sequence
126700
-
calculated from amino acid sequence
146000
-
gel filtration
160000
171000
-
with His6-tagged alpha subunits, gel filtration, sucrose density gradient
175000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
when the E1alpha subunit is fully phosphorylated, overall BCKDC activity is zero
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method using 25-26% (v/v) PEG 200 in 0.1 M MES buffer pH 6.2 as a precipitant
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
rapid inactivation at pH 4
677424
5 - 7
-
stable at pH 5-7
677424
8
-
inactivation at pH 8
677424
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
sufficiently stable up to 40C, but rapidly loses activity at higher temperatures
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DMSO
-
completely stable in the presence of 20% (v/v) DMSO (half-life: 150 h)
polyethyleneglycol
-
rapidly inactivated in the presence of 15% (v/v) PEG-400
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
anion exchange chromatography and gel filtration
immobilized metal chelate chromatography and gel filtration
-
Ni-NTA column chromatography
-
nickel-charged metal chelating column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli Rosetta 2 (DE3) and various Escherichia coli strains
expressed in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli strain H-81
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A240P-alpha
-
slow assembly of alpha2beta2 tetramer
D295A
-
of component E1b, 2fold increase in kcat-value
E193A-alpha
-
complete inactivation of enzyme
E76A-beta
-
complete inactivation of enzyme
F364C-alpha
-
slow assembly of enzyme, alphabeta dimer
G204S-alpha
-
slow assembly of alpha2beta2 tetramer
G245R-alpha
-
moderately slow assembly of alpha2beta2 tetramer
H146A-beta
-
complete inactivation of enzyme
H291A-alpha
-
partially active enzyme
N222S-alpha
R114W-alpha
-
naturally occuring mutation in maple syrup disease patients, strongly reduced binding of thiamin diphosphate, enzyme inactive
R220W-alpha
R287A
-
of component E1b, 40fold increase in Km-value for 2-oxoisovalerate
R301A
-
of component E1b, 4fold increase in Km-value for 2-oxoisovalerate
T166M-alpha
-
enzyme inactive, with attenuated ability to bind thiamin diphosphate
T265R
-
no assembly of alpha2beta2 tetramer
Y224A-alpha
-
markedly higher Km value for thiamin diphosphate
Y300A
-
of component E1b, 6fold increase in Km-value for 2-oxoisovalerate
Y300F
-
of component E1b, 5fold increase in Km-value for 2-oxoisovalerate
Y368C-alpha
-
slow assembly of enzyme as alphabeta dimer and alpha2beta2 tetramer
Y393N-alpha
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
after denaturation in 8 M urea, reconstitution at 23C with absolute requirement of chaperonins GroEL/GroES and MgATP2-
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
plants with enzymic activity show enhanced cold tolerance, role as a protective mechanism for growth of plants under sub optimal temperatures
medicine
synthesis
-
the enzyme is able to catalyze carboligation reactions with an exceptionally broad substrate range, a feature that makes KdcA a potentially valuable biocatalyst for C-C bond formation, in particular for the enzymatic synthesis of diversely substituted 2-hydroxyketones with high enantioselectivity