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Information on EC 1.3.8.4 - isovaleryl-CoA dehydrogenase and Organism(s) Rattus norvegicus and UniProt Accession P12007
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1.3.8.4 isovaleryl-CoA dehydrogenaseIUBMB Comments
Contains FAD as prosthetic group. Pentanoate can act as donor.
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Word Map
- 1.3.8.4
-
acidemia
- acyl-coa
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inborn
- 3-methylcrotonyl-coa
-
isovalerylglycine
-
medium-chain
-
lethargy
-
flavoenzyme
- isobutyryl-coa
- acylcarnitine
- isovalerylcarnitine
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flavoprotein:ubiquinone
- glutaryl-coa
- 2-methylbutyryl-coa
-
3-hydroxyisovaleric
- octanoyl-coa
-
sweaty
- diagnostics
- medicine
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
isovaleryl-coa dehydrogenase, isovaleryl-coenzyme a dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
isovaleroyl-coenzyme A dehydrogenase
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-
-
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isovaleryl-coenzyme A dehydrogenase
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-
-
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IVD
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
-
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oxidation
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-
-
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
3-methylbutanoyl-CoA:electron-transfer flavoprotein oxidoreductase
Contains FAD as prosthetic group. Pentanoate can act as donor.
CAS REGISTRY NUMBER
COMMENTARY
37274-61-6
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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
(S)-2-methylbutyryl-CoA + electron-transfer flavoprotein
2-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
butyryl-CoA + electron-transfer flavoprotein
crotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
hexanoyl-CoA + electron-transfer flavoprotein
hex-2-enoyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
butyryl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
-
3.3% relative activity to isovaleryl-CoA
-
?
isovaleryl-CoA + phenazine methosulfate
3-methylcrotonyl-CoA + reduced phenazine methosulfate
-
-
-
-
?
isovaleryl-CoA + FAD
3-methylcrotonyl-CoA + FADH2
with ferrocenium hexafluorophosphate as second electron acceptor
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
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-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
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isovaleryl-CoA is the preferred substrate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
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isovaleryl-CoA is the preferred substrate
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?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
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isovaleryl-CoA is the preferred substrate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
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acceptors: electron-transfer flavoprotein, phenazine methosulfate
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?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
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acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
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electron acceptor: electron-transfer flavoprotein serves as a natural electron acceptor for the enzyme with isovaleryl-CoA as substrate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
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electron acceptor: electron-transfer flavoprotein serves as a natural electron acceptor for the enzyme with isovaleryl-CoA as substrate
-
?
n-valeryl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
-
-
-
?
n-valeryl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
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-
-
?
n-valeryl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
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32% relative specific activity to isovaleryl-CoA
-
?
additional information
?
-
the enzyme catalyzes the dehydrogenation of monomethyl branched-chain fatty acid thioester derivatives
-
-
?
additional information
?
-
broader substrate specificity, overview. The enzyme is also active with octanoyl-CoA, decanoyl-CoA, and dodecanoyl-CoA. No activity with isobutyryl-CoA and myristoyl-CoA, with DCIPIP and phenazine methosulfate as second electron acceptors
-
-
?
additional information
?
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the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
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
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
electron acceptor: electron-transfer flavoprotein serves as a natural electron acceptor for the enzyme with isovaleryl-CoA as substrate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
electron acceptor: electron-transfer flavoprotein serves as a natural electron acceptor for the enzyme with isovaleryl-CoA as substrate
-
?
additional information
?
-
the enzyme catalyzes the dehydrogenation of monomethyl branched-chain fatty acid thioester derivatives
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
the enzyme contains FAD as a prosthetic group, 0.6 mol FAD per mol of subunit
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hypoglycin
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inhibits, induces isovaleric acidemia when administered in experimental animals
p-hydroxymercuribenzoate
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completely inhibits at a concentration of 0.01 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0113
isovaleryl-CoA
-
purified enzyme in the absence of electron transfer agents
0.0132
isovaleryl-CoA
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purified enzyme with electron-transferring flavoprotein and dichlorophenol indophenol, reaction terminated with KMnO4/HCl
0.0208
isovaleryl-CoA
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purified enzyme with phenazine methosulfate and dichlorophenol indophenol, reaction terminated with KMnO4/HCl
0.033
isovaleryl-CoA
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with phenazine methosulfate as an artificial electron acceptor
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
(S)-2-methylbutyryl-CoA
wild-type enzyme and mutant IVD G375E, pH 7.4, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
inhibition kinetics, overview
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00044
-
sonicated mitochondria, acceptor added: electron-transferring flavoprotein
0.086
0.832
2.68
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). IVD_RAT
424
0
46435
Swiss-Prot
Mitochondrion (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E254G/G375E
site-directed mutagenesis, shows no activity with (S)-2-methylbutyryl-CoA in contrast to the wild-type enzyme, reduced activity compared to the wild-type enzyme
G375E
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using sonication, ammonium sulfate treatment and column chromatography on DEAE-Sephadex A-50, hydroxylapatite, Matrex Gel Blue A and BioGel A-0.5 m
-
using sonication, ammonium sulfate treatment, column chromatography on DEAE-Sephadex A-50, hydroxylapatite and isoelectrofocusing
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and comparison, expression in Escherichia coli strain BL21(DE3)
via immunopurification of enzyme mRNA from polyribosomes for preparation of an enriched cDNA library in pBR322 plasmid, and screening with synthetic oligonucleotide probes corresponding to the amino-terminal sequence of purified rat enzyme protein
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Matsubara, Y.; Indo, Y.; Naito, E.; Ozasa, H.; Glassberg, R.; Vockley, J.; Ikeda, Y.; Kraus, J.; Tanaka, K.
Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family
J. Biol. Chem.
264
16321-16331
1989
Rattus norvegicus
Ikeda, Y.; Tanaka, K.
Isovaleryl-CoA dehydrogenase from rat liver
Methods Enzymol.
166
374-389
1988
Rattus norvegicus
Ikeda, Y.; Tanaka, K.
Purification and characterization of isovaleryl coenzyme A dehydrogenase from rat liver mitochondria
J. Biol. Chem.
258
1077-1085
1983
Rattus norvegicus
Ikeda, Y.; Dabrowski, C.; Tanaka, K.
Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria. Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase
J. Biol. Chem.
258
1066-1076
1983
Rattus norvegicus
Rhead, W.J.; Hall, C.; Tanaka, K.
Novel tritium release assays for isovaleryl-CoA and butyryl-CoA dehydrogenases
J. Biol. Chem.
256
1616-1624
1981
Cavia porcellus, Rattus norvegicus
Noda, C.; Rhead, W.J.; Tanaka, K.
Isovaleryl-CoA dehydrogenase: demonstration in rat liver mitochondria by ion exchange chromatography and isoelectric focusing
Proc. Natl. Acad. Sci. USA
77
2646-2650
1980
Rattus norvegicus
Osmundsen, H.; Billington, D.; Sherrat, H.S.A.
Evidence for a separate isovaleryl-coenzyme A dehydrogenase in liver mitochondria
Biochem. Soc. Trans.
2
1286-1288
1974
Rattus norvegicus
-
Tanaka, K.; Miller, E.M.; Isselbacher, K.J.
Hypoglycin A: a specific inhibitor of isovaleryl CoA dehydrogenase
Proc. Natl. Acad. Sci. USA
68
20-24
1971
Rattus norvegicus
Liu, X.; Wu, L.; Deng, G.; Chen, G.; Li, N.; Chu, X.; Li, D.
Comparative studies of acyl-CoA dehydrogenases for monomethyl branched chain substrates in amino acid metabolism
Bioorg. Chem.
47
1-8
2013
Rattus norvegicus (P12007)
Luis, P.B.; Ruiter, J.P.; Ijlst, L.; Tavares de Almeida, I.; Duran, M.; Mohsen, A.W.; Vockley, J.; Wanders, R.J.; Silva, M.F.
Role of isovaleryl-CoA dehydrogenase and short branched-chain acyl-CoA dehydrogenase in the metabolism of valproic acid: implications for the branched-chain amino acid oxidation pathway
Drug Metab. Dispos.
39
1155-1160
2011
Rattus norvegicus (P12007)
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