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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 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.8 With a flavin as acceptor
                1.3.8.4 isovaleryl-CoA dehydrogenase
IUBMB Comments
Contains FAD as prosthetic group. Pentanoate can act as donor.
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This record set is specific for:
Rattus norvegicus
UNIPROT: P12007
Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Synonyms
isovaleryl-coa dehydrogenase, sbcad, short/branched chain acyl-coa dehydrogenase, isovaleryl-coenzyme a dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isovaleroyl-coenzyme A dehydrogenase
-
-
-
0
isovaleryl-coenzyme A dehydrogenase
-
-
-
0
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
0
oxidation
-
-
-
0
reduction
-
-
-
0
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 hide
37274-61-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-2-methylbutyryl-CoA + electron-transfer flavoprotein
2-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
-
-
-
?
butyryl-CoA + electron-transfer flavoprotein
crotonyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
-
-
-
?
hexanoyl-CoA + electron-transfer flavoprotein
hex-2-enoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
-
-
-
?
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
-
-
-
?
isovaleryl-CoA + FAD
3-methylcrotonyl-CoA + FADH2
show the reaction diagram
butyryl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
show the reaction diagram
-
3.3% relative activity to isovaleryl-CoA
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
show the reaction diagram
isovaleryl-CoA + phenazine methosulfate
3-methylcrotonyl-CoA + reduced phenazine methosulfate
show the reaction diagram
-
-
-
-
?
n-valeryl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
-
-
-
?
isovaleryl-CoA + FAD
3-methylcrotonyl-CoA + FADH2
show the reaction diagram
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
electron transferring flavoprotein
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
valproyl-CoA
competitive
valproyl-dephosphoCoA
competitive
(methylenecyclopropyl)acetyl-CoA
3-methylcrotonyl-CoA
-
-
Ag+
-
completely inhibits at 0.01 mM
alpha-keto-methylenecyclopropylpropionic acid
-
-
Cu2+
-
completely inhibits at 0.01 mM
Hg2+
-
completely inhibits at 0.1 mM
hypoglycin
Methylmercury iodide
N-ethylmaleimide
p-hydroxymercuribenzoate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0019 - 0.0035
(S)-2-methylbutyryl-CoA
0.0029 - 0.125
isovaleryl-CoA
0.00043
FAD
-
-
0.0063 - 0.033
isovaleryl-CoA
0.0167 - 0.4
n-valeryl-CoA
0.51
phenazine methosulfate
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
(S)-2-methylbutyryl-CoA
wild-type enzyme and mutant IVD G375E, pH 7.4, 37°C
0.17 - 1.5
isovaleryl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.086 - 0.16
(S)-2-methylbutyryl-CoA
0.045 - 0.53
isovaleryl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.074
valproyl-CoA
versus isovaleryl-CoA, pH 8.0, 37°C
0.17
valproyl-dephosphoCoA
versus isovaleryl-CoA, pH 8.0, 37°C
0.02
3-methylcrotonyl-CoA
-
-
additional information
additional information
inhibition kinetics, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00003
-
intact mitochondria, no added acceptor
0.00016
-
sonicated mitochondria, no added acceptor
0.00044
-
sonicated mitochondria, acceptor added: electron-transferring flavoprotein
0.00046
-
sonicated mitochondria, acceptor added: phenazine methosulfate
0.005
-
sonicate
0.012
-
Triton X-100 extract
0.0125
-
sonicate supernatant fraction
0.014
-
soluble extract
0.086
0.832
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
isovaleryl-CoA + phenazine methosulfate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to acyl-CoA dehydrogenase (ACD) family
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
IVD_RAT
424
0
46435
Swiss-Prot
Mitochondrion (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
175000
-
gel filtration
43000
-
4 * 43000, SDS-PAGE
43098
-
4 * 43098, nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E254G
site-directed mutagenesis, inactive mutant
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
-20°C, 50% glycerol, 1 month
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using ion exchange column chromatography and isoelectric focusing
-
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
-
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
Manually annotated by BRENDA team
Ikeda, Y.; Tanaka, K.
Isovaleryl-CoA dehydrogenase from rat liver
Methods Enzymol.
166
374-389
1988
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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