Information on EC 1.3.99.12 - 2-methylacyl-CoA dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.3.99.12
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RECOMMENDED NAME
GeneOntology No.
2-methylacyl-CoA dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-methylbutanoyl-CoA + acceptor = 2-methylbut-2-enoyl-CoA + reduced acceptor
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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redox reaction
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-
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reduction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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Metabolic pathways
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Valine, leucine and isoleucine degradation
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valine metabolism
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SYSTEMATIC NAME
IUBMB Comments
2-methylbutanoyl-CoA:acceptor oxidoreductase
Also oxidizes 2-methylpropanoyl-CoA. Not identical with EC 1.3.8.1 (butyryl-CoA dehydrogenase), EC 1.3.8.7 (medium-chain acyl-CoA dehydrogenase), EC 1.3.8.8 (long-chain acyl-CoA dehydrogenase), EC 1.3.8.9 (very-long-chain acyl-CoA dehydrogenase) or EC 1.3.99.10 (isovaleryl-CoA dehydrogenase).
CAS REGISTRY NUMBER
COMMENTARY hide
85130-32-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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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
(R)-2-methylbutanoyl-CoA + acceptor
2-methylbut-2-enoyl-CoA + reduced acceptor
show the reaction diagram
(R)-2-methylbutyryl-CoA + acceptor
2-ethylprop-2-enoyl-CoA + reduced acceptor
show the reaction diagram
(S)-2-methylbutanoyl-CoA + acceptor
2-methylbut-2-enoyl-CoA + reduced acceptor
show the reaction diagram
2-methylbutanoyl-CoA + acceptor
2-methylbut-2-enoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
2-methylbutanoyl-CoA + electron transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron transfer flavoprotein
show the reaction diagram
2-methylpentanoyl-CoA + acceptor
2-methyl-2-pentenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
butyryl-CoA + acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
butyryl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
hexanoyl-CoA + acceptor
hex-2-enoyl-CoA + reduced acceptor
show the reaction diagram
isobutyryl-CoA + acceptor
2-methylacryloyl-CoA + reduced acceptor
show the reaction diagram
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6% of activity with (S)-2-methylbutanoyl-CoA
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-
?
isobutyryl-CoA + acceptor
isobutyr-2-yl-CoA + reduced acceptor
show the reaction diagram
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37% of activity with (S)-2-methylbutanoyl-CoA, wild-type enzyme
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-
?
isobutyryl-CoA + acceptor
methacrylyl-CoA + reduced acceptor
show the reaction diagram
octanoyl-CoA + acceptor
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
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13-14% of activity with 2-methylbutyryl-CoA
-
?
octanoyl-CoA + acceptor
oct-2-enoyl-CoA + reduced acceptor
show the reaction diagram
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-
-
-
?
pentanoyl-CoA + acceptor
2-pentenoyl-CoA + reduced acceptor
show the reaction diagram
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13-14% of activity with 2-methylbutyryl-CoA
-
?
valeryl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
additional information
?
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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
(R)-2-methylbutanoyl-CoA + acceptor
2-methylbut-2-enoyl-CoA + reduced acceptor
show the reaction diagram
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involved in the (S)-pathway of L-isoleucine oxidation, and also in the (R)-pathway of L-alloisoleucine oxidation due to interconvertion of the 3 isomers
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-
?
(S)-2-methylbutanoyl-CoA + acceptor
2-methylbut-2-enoyl-CoA + reduced acceptor
show the reaction diagram
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involved in the (S)-pathway of L-isoleucine oxidation, and also in the (R)-pathway of L-alloisoleucine oxidation due to interconvertion of the 3 isomers
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?
2-methylbutanoyl-CoA + electron transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron transfer flavoprotein
show the reaction diagram
additional information
?
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enzyme deficiency causes 2-ethylhydracrylic aciduria with excretion f 2-methylbutyrylglycine
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(Methylenecyclopropyl)acetyl-CoA
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0.0025 mM, slow inhibition, half-time approx. 30 min
2-butenoyl-CoA
2-methylbut-2-enoyl-CoA
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acetoacetyl-CoA
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butyryl-CoA
decanoyl-CoA
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Hexanoyl-CoA
Methylmercury iodide
N-ethylmaleimide
p-hydroxymercuribenzoate
pentanoyl-CoA
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0.1 mM, 50% inhibition
tiglyl-CoA
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0011 - 0.0107
(S)-2-methylbutanoyl-CoA
0.001
2-methylbutanoyl-CoA
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recombinant enzyme, 32C
0.018 - 0.02
2-methylbutyryl-CoA
0.021
2-Methylvaleryl-CoA
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-
0.00051
FAD
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0.0053 - 0.15
Hexanoyl-CoA
0.026 - 0.13
isobutyryl-CoA
0.48
phenazine methosulfate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1200 - 9700
(S)-2-methylbutanoyl-CoA
1.77
2-methylbutanoyl-CoA
Solanum tuberosum
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per enzyme tetramer, recombinant enzyme, 32C
1200 - 7600
Hexanoyl-CoA
2000 - 8500
isobutyryl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.115
2-butenoyl-CoA
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-
0.003 - 0.011
2-methylbut-2-enoyl-CoA
0.00006
acetoacetyl-CoA
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(S)-2-methylbutyryl-CoA as substrate
0.00004
decanoyl-CoA
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(S)-2-methylbutyryl-CoA as substrate
0.016
Hexanoyl-CoA
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(S)-2-methylbutyryl-CoA as substrate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.618
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28
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recombinant wild-type enzyme, substrate (S)-2-methylbutanoyl-CoA
35
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recombinant wild-type enzyme, substrate (S)-2-methylbutanoyl-CoA
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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2-methylbutyryl-CoA + Medola's Blue
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41500
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4 * 41500, SDS-PAGE
42500
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4 * 42500, SDS-PAGE
50000
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4 * 50000, about, SDS-PAGE
170000
188000
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recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, pH 7.4, 10% glycerol, 1 month, no loss in activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant from Escherichia coli to over 90% purity
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recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain XL1Blue
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expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A383T
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site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
E107D/L112V/T115K/I117K
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site-directed mutagenesis, mutant is not stable
F105L
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site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
L220M/A383T
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site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
L220M/L222I
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site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
L220M/L222I/A383T
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site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
L222I/A383T
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site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
S177N
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site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
V104L
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site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
V104L/F105L
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site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
additional information
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construction of deletion mutants, substrate specificity and catalytic efficiency, overview