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Information on EC 1.3.8.4 - isovaleryl-CoA dehydrogenase and Organism(s) Homo sapiens and UniProt Accession P26440
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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
-
inborn
- 3-methylcrotonyl-coa
-
isovalerylglycine
-
medium-chain
-
lethargy
-
flavoenzyme
- isobutyryl-coa
- acylcarnitine
- isovalerylcarnitine
-
flavoprotein:ubiquinone
- glutaryl-coa
- 2-methylbutyryl-coa
-
3-hydroxyisovaleric
- octanoyl-coa
-
sweaty
- diagnostics
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
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
-
-
-
-
isovaleryl-coenzyme A dehydrogenase
-
-
-
-
IVD
IVD
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
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
-
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
isovaleryl-CoA + electron transfer protein
3-methylcrotonoyl-CoA + reduced electron transfer protein
acceptor porcine electron transfer protein
-
-
?
2-methylbutanoyl-CoA + acceptor
2-methylbut-2-enoyl-CoA + reduced acceptor
-
low activity with the wild-type and mutant L95V/A99V/L103V/L370M/G374A
-
-
?
isovaleryl-CoA + electron transfer protein
3-methylcrotonoyl-CoA + reduced electron transfer protein
-
-
-
-
?
isovaleryl-CoA + electron transfer protein
3-methylcrotonyl-CoA + reduced electron transfer protein
-
-
-
-
?
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
-
r
isovaleryl-CoA + phenazine methosulfate
3-methylcrotonyl-CoA + reduced phenazine methosulfate
-
-
-
-
?
n-valeryl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
-
46% relative specific activity to isovaleryl-CoA
-
?
octanoyl-CoA + acceptor
oct-2-enoyl-CoA + reduced acceptor
-
1% relative specific activity to isovaleryl-CoA
-
?
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-transferring flavoprotein, dichlorophenol indophenol or dichlorophenol indophenol + FAD
-
?
butyryl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
-
acceptor: phenazine methosulfate
-
?
butyryl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
-
21% relative specific activity to isovaleryl-CoA
-
?
hexanoyl-CoA + acceptor
hex-2-enoyl-CoA + reduced acceptor
-
acceptor: phenazine methosulfate
-
?
hexanoyl-CoA + acceptor
hex-2-enoyl-CoA + reduced acceptor
-
15% relative specific activity to isovaleryl-CoA
-
?
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
-
the catalytic activity of the recombinant wild-type enzyme is the highest in the presence of isovaleryl-CoA
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
electron acceptor: electron-transferring flavoprotein
-
?
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
-
?
additional information
?
-
deficiency of the enzyme in humans is responsible for isovaleric acidemia
-
-
?
additional information
?
-
-
deficiency of the enzyme in humans is responsible for isovaleric acidemia
-
-
?
additional information
?
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
-
substrate specificity of wild-type and mutant enzymes
-
-
?
additional information
?
-
-
deficiency of the enzyme in humans is responsible for isovaleric acidemia
-
-
?
additional information
?
-
-
E254 of the enzyme is in close proximity to the bound FAD, E254 is the active site catalytic residue
-
-
?
additional information
?
-
-
E254 of the enzyme is in close proximity to the bound FAD, E254 is the active site catalytic residue
-
-
?
additional information
?
-
-
the location of the catalytic residue together with a glycine at position 374 is important for conferring branched-chain substrate specificity to the enzyme
-
-
?
additional information
?
-
-
R387 has an important role in anchoring the substrate
-
-
?
additional information
?
-
-
the type III enzyme mutation responsible for isovaleric acidemia leads to a shift in reading frame and the subsequent incorporation of eight abnormally placed amino acids with premature termination of translation
-
-
?
additional information
?
-
-
a specific deficiency of enzyme activity is observed in cultured skin fibroblasts from patients with isovaleric acidemia
-
-
?
additional information
?
-
-
a specific deficiency of enzyme activity is observed in cultured skin fibroblasts from patients with isovaleric acidemia
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
-
physiological implications of enzyme mutations and deficiency
-
-
?
additional information
?
-
-
isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency
-
-
?
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 + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
?
isovaleryl-CoA + electron transfer protein
3-methylcrotonoyl-CoA + reduced electron transfer protein
-
-
-
-
?
isovaleryl-CoA + electron transfer protein
3-methylcrotonyl-CoA + reduced electron transfer protein
-
-
-
-
?
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
-
-
-
?
additional information
?
-
deficiency of the enzyme in humans is responsible for isovaleric acidemia
-
-
?
additional information
?
-
-
deficiency of the enzyme in humans is responsible for isovaleric acidemia
-
-
?
additional information
?
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
-
deficiency of the enzyme in humans is responsible for isovaleric acidemia
-
-
?
additional information
?
-
-
E254 of the enzyme is in close proximity to the bound FAD, E254 is the active site catalytic residue
-
-
?
additional information
?
-
-
E254 of the enzyme is in close proximity to the bound FAD, E254 is the active site catalytic residue
-
-
?
additional information
?
-
-
the location of the catalytic residue together with a glycine at position 374 is important for conferring branched-chain substrate specificity to the enzyme
-
-
?
additional information
?
-
-
R387 has an important role in anchoring the substrate
-
-
?
additional information
?
-
-
the type III enzyme mutation responsible for isovaleric acidemia leads to a shift in reading frame and the subsequent incorporation of eight abnormally placed amino acids with premature termination of translation
-
-
?
additional information
?
-
-
a specific deficiency of enzyme activity is observed in cultured skin fibroblasts from patients with isovaleric acidemia
-
-
?
additional information
?
-
-
a specific deficiency of enzyme activity is observed in cultured skin fibroblasts from patients with isovaleric acidemia
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
-
physiological implications of enzyme mutations and deficiency
-
-
?
additional information
?
-
-
isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
RYATLPNIMKAK
twelvemer peptide representing the electron transfer protein docking peptide, ETF betaArg191-betaLys202, competitively inhibits the enzyme reaction when electron transfer protein is used as the electron acceptor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0028
isovaleryl-CoA
purified V342A mutant, electron acceptor: electron-transferring flavoprotein
0.0031
isovaleryl-CoA
purified wild-type enzyme, electron acceptor: electron-transferring flavoprotein
0.0045
isovaleryl-CoA
purified R382L mutant, electron acceptor: dichlorophenol indophenol
0.0069
isovaleryl-CoA
purified R382L mutant, electron acceptor: electron-transferring flavoprotein
0.024
isovaleryl-CoA
purified V342A mutant, electron acceptor: dichlorophenol indophenol
0.027
isovaleryl-CoA
purified A282V mutant, electron acceptor: electron-transferring flavoprotein
0.0296
isovaleryl-CoA
purified wild-type enzyme, electron acceptor: dichlorophenol indophenol
0.41
isovaleryl-CoA
purified A282V mutant, electron acceptor: dichlorophenol indophenol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.283
isovaleryl-CoA
purified V342A mutant, electron acceptor: dichlorophenol indophenol
0.733
isovaleryl-CoA
purified R382L mutant, electron acceptor: dichlorophenol indophenol
0.817
isovaleryl-CoA
purified V342A mutant, electron acceptor: electron-transferring flavoprotein
2
isovaleryl-CoA
purified R382L mutant, electron acceptor: electron-transferring flavoprotein
2.2
isovaleryl-CoA
purified A282V mutant, electron acceptor: electron-transferring flavoprotein
2.82
isovaleryl-CoA
purified A282V mutant, electron acceptor: dichlorophenol indophenol
8.8
isovaleryl-CoA
purified wild-type enzyme, electron acceptor: electron-transferring flavoprotein
10
isovaleryl-CoA
purified wild-type enzyme, electron acceptor: dichlorophenol indophenol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00034
fibroblast cell line harboring the mutation corresponding to the A282V mutant
0.004
cell free extract of Escherichia coli cells expressing the enzyme mutant R363C
0.032
cell free extract of Escherichia coli cells expressing the enzyme mutant R382L
0.052
cell free extract of Escherichia coli cells expressing the enzyme mutant V342A
0.086
cell free extract of Escherichia coli cells expressing the enzyme mutant A282V
0.44
cell free extract of Escherichia coli cells expressing the enzyme, wild type
0.6
of purified recombinant V342A mutant, electron acceptor: electron-transferring flavoprotein
1.24
of purified recombinant V342A mutant, electron acceptor: dichlorophenol indophenol + FAD
1.27
of purified recombinant V342A mutant, electron acceptor: dichlorophenol indophenol
1.4
of purified recombinant R382L mutant, electron acceptor: electron-transferring flavoprotein
10.3
of purified recombinant wild-type enzyme, electron acceptor: dichlorophenol indophenol + FAD
11.7
of purified recombinant wild-type enzyme, electron acceptor: electron-transferring flavoprotein
2.04
of purified recombinant A282V mutant, electron acceptor: dichlorophenol indophenol
2.2
of purified recombinant A282V mutant, electron acceptor: electron-transferring flavoprotein
2.33
of purified recombinant A282V mutant, electron acceptor: dichlorophenol indophenol + FAD
4.88
of purified recombinant R382L mutant, electron acceptor: dichlorophenol indophenol
6.34
of purified recombinant R382L mutant, electron acceptor: dichlorophenol indophenol + FAD
8.2
of purified recombinant wild-type enzyme, electron acceptor: dichlorophenol indophenol
0.000039
-
mitochondria from isovaleric acidemia cells, 13% relative activity to normal cells, specific activity determined by tritium release assay
0.000163
-
mitochondria from isovaleric acidemia cells, 12% relative activity to normal cells, specific activity determined by dye reduction assay
0.0003
-
recombinant mutant L95V/A99V/L103V/L370M/G374A, substrate 2-methylbutanoyl-CoA
0.00031
-
mitochondria from normal cells, specific activity determined by tritium release assay
0.00131
-
mitochondria from normal cells, specific activity determined by dye reduction assay
0.01
-
propionyl-CoA as substrate and phenazine methosulfate as acceptor or hexanoyl-CoA as substrate and 0.0056 mM electron transfer flavoprotein as acceptor
0.03
-
butyryl-CoA as substrate and 0.0056 mM electron transfer flavoprotein as acceptor
0.09
-
valeryl-CoA as substrate and 0.0056 mM electron transfer flavoprotein as acceptor
0.17
-
S-2-methylbutyryl-CoA as substrate and phenazine methosulfate as acceptor
0.53
-
isovaleryl-CoA as substrate and 0.0056 mM electron transfer flavoprotein as acceptor
0.72
-
isovaleryl-CoA as substrate and 0.012 mM electron transfer flavoprotein as acceptor
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
malfunction
-
deficiency in isovaleryl-CoA dehydrogenase causes isovaleric acidemia, a rare inherited metabolic disease
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_HUMAN
426
0
46651
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
initial crystallization performed by vapor diffusion using the hanging drop method following the sparse matrix protocol, final crystallization condition involves vapor diffusion using both hanging and sitting drop techniques, enzyme expressed in Escherichia coli crystallizes in the orthorhombic space group P212121 with unit cell parameters a: 94 A, b: 97.7 A, and c: 181.7 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y166F
mutation does not block enzyme interaction with the electron transfer protein
A282V
-
site-directed mutagenesis, severely affected interaction between enzyme and flavin cofactor, about 40% reduced activity compared to the wild-type enzyme
C30Y
-
isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency. Molecular analysis of their IVD gene reveals six mutation profiles: R21H, R363C, H100R, S97F, C30Y and Y371C (common recurring missense mutation)
E254G
H100R
-
isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency. Molecular analysis of their IVD gene reveals six mutation profiles: R21H, R363C, H100R, S97F, C30Y and Y371C (common recurring missense mutation)
I199M
-
naturally occuring missense mutation in a Chinese infant, G39A genotype, phenotype, overview
L370M/G374A
-
site-directed mutagenesis, substrate specificity similar to the wild-type enzyme, reduced activity
L95V/A99V/L103V/L370M/G374A
-
site-directed mutagenesis, substitutions in the human enzyme mimick the potato isovaleryl-CoA dehydrogenase isozyme 1, which shows major 2-methylbutyryl-CoA dehydrogenase activity and rather belongs to EC 1.3.99.12, the mutant enzymes shows modified substrate specificty and also exhibits highest activity with 2-methylbutanoyl-CoA, molecular modeling of the active site
R21H
-
isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency. Molecular analysis of their IVD gene reveals six mutation profiles: R21H, R363C, H100R, S97F, C30Y and Y371C (common recurring missense mutation)
R363C
-
isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency. Molecular analysis of their IVD gene reveals six mutation profiles: R21H, R363C, H100R, S97F, C30Y and Y371C (common recurring missense mutation)
R387A
-
enzyme activity detected, the mutant is less able than the mutant R387K to properly form the charge-transfer complex intermediate
R387E
-
enzyme activity detected, the mutant is less able than the mutant R387K to properly form the charge-transfer complex intermediate
R387K
-
enzyme activity detected, the mutant is able to form the charge-transfer complex intermediate with similar efficiency to wild-type
R387Q
-
enzyme activity detected, the mutant is less able than the mutant R387K to properly form the charge-transfer complex intermediate
S97F
-
isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency. Molecular analysis of their IVD gene reveals six mutation profiles: R21H, R363C, H100R, S97F, C30Y and Y371C (common recurring missense mutation)
W13X
-
naturally occuring missense mutation in a Chinese infant, C597G genotype, phenotype, overview. The mutation may destabilize the IVD monomer structure and affect the interaction between IVD and flavin adenine dinucleotide
Y371C
-
isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency. Molecular analysis of their IVD gene reveals six mutation profiles: R21H, R363C, H100R, S97F, C30Y and Y371C (common recurring missense mutation)
E254G
-
no activity, mutant enzyme is unable to form a charge-transfer complex with substrate/product. The CD spectra indicate a perturbation of the flavin environment
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by loading the supernatant from an induced culture onto an XK16/20 Fast Q fast flow column, overnight dialysis in potassium phosphate buffer, and hydroxyapatite column chromatography
using ammonium sulfate fractionation followed by DEAE-Sephadex A-50, hydroxyapatite, Matrex Gel Blue A, agarose-hexane-CoA, and Bio-Gel A-0.5 column chromatography
-
using bacterial lysates through centrifugation, filtration through an Acrodisc filter, chromatography on a XK16/20 DEAE fast-flow column and hydroxyapatite resin column
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA modified at its 5'-end coding region to enhance expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
diagnostics
-
enzyme activity assay development for determination of isovaleric acidemia in newborn disorder screening
medicine
isovaleric acidemia is caused by isovaleryl-CoA dehydrogenase deficiency
medicine
isovaleric acidaemia, caused by isovaleryl coenzyme A dehydrogenase deficiency, is an autosomal-recessive disorder of L-leucine catabolism
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Finocchiaro, G.; Ito, M.; Tanaka, K.
Purification and properties of short chain acyl-CoA, medium chain acyl-CoA, and isovaleryl-CoA dehydrogenases from human liver
J. Biol. Chem.
262
7982-7989
1987
Homo sapiens
Rhead, W.J.; Tanaka, K.
Demonstration of a specific mitochondrial isovaleryl-CoA dehydrogenase deficiency in fibroblasts from patients with isovaleric acidemia
Proc. Natl. Acad. Sci. USA
77
580-583
1980
Homo sapiens
Mohsen, A.W.A.; Vockley, J.
Identification of the active site catalytic residue in human isovaleryl-CoA dehydrogenase
Biochemistry
34
10146-10152
1995
Homo sapiens
Tiffany, K.A.; Roberts, D.L.; Wang, M.; Paschke, R.; Mohsen, A.W.A.; Vockley, J.; Kim, J.J.P.
Structure of human isovaleryl-CoA dehydrogenase at 2.6 ANG resolution: Structural basis for substrate specificity
Biochemistry
36
8455-8464
1997
Homo sapiens
Mohsen, A.W.A.; Anderson, B.D.; Volchenboum, S.L.; Battaile, K.P.; Tiffany, K.; Roberts, D.; Kim, J.J.P.; Vockley, J.
Characterization of molecular defects in isovaleryl-CoA dehydrogenase in patients with isovaleric acidemia
Biochemistry
37
10325-10335
1998
Homo sapiens (P26440), Homo sapiens
Volchenboum, S.L.; Vockley, J.
Mitochondrial import and processing of wild type and type III mutant isovaleryl-CoA dehydrogenase
J. Biol. Chem.
275
7958-7963
2000
Homo sapiens
Volchenboum, S.L.; Mohsen, A.W.A.; Kim, J.J.P.; Vockley, J.
Arginine 387 of human isovaleryl-CoA dehydrogenase plays a crucial role in substrate/product binding
Mol. Genet. Metab.
74
226-237
2001
Homo sapiens
Nasser, I.; Mohsen, A.W.; Jelesarov, I.; Vockley, J.; Macheroux, P.; Ghisla, S.
Thermal unfolding of medium-chain acyl-CoA dehydrogenase and iso(3)valeryl-CoA dehydrogenase: study of the effect of genetic defects on enzyme stability
Biochim. Biophys. Acta
1690
22-32
2004
Homo sapiens
Tajima, G.; Sakura, N.; Yofune, H.; Dwi Bahagia Febriani, A.; Nishimura, Y.; Sakamoto, A.; Ono, H.; Shigematsu, Y.; Kobayashi, M.
Establishment of a practical enzymatic assay method for determination of isovaleryl-CoA dehydrogenase activity using high-performance liquid chromatography
Clin. Chim. Acta
353
193-199
2005
Homo sapiens
Goetzman, E.S.; Mohsen, A.W.; Prasad, K.; Vockley, J.
Convergent evolution of a 2-methylbutyryl-CoA dehydrogenase from isovaleryl-CoA dehydrogenase in Solanum tuberosum
J. Biol. Chem.
280
4873-4879
2005
Homo sapiens, Solanum tuberosum (Q9FS87), Solanum tuberosum
Goetzman, E.S.; He, M.; Nguyen, T.V.; Vockley, J.
Functional analysis of acyl-CoA dehydrogenase catalytic residue mutants using surface plasmon resonance and circular dichroism
Mol. Genet. Metab.
87
232-242
2006
Homo sapiens
-
Lin, W.D.; Wang, C.H.; Lee, C.C.; lai, C.C.; Tsai, Y.; Tsai, F.J.
Genetic mutation profile of isovaleric acidemia patients in Taiwan
Mol. Genet. Metab.
90
134-139
2007
Homo sapiens
Lee, Y.W.; Lee, D.H.; Vockley, J.; Kim, N.D.; Lee, Y.K.; Ki, C.S.
Different spectrum of mutations of isovaleryl-CoA dehydrogenase (IVD) gene in Korean patients with isovaleric acidemia
Mol. Genet. Metab.
92
71-77
2007
Homo sapiens (P26440), Homo sapiens
Bonilla Guerrero, R.; Wolfe, L.A.; Payne, N.; Tortorelli, S.; Matern, D.; Rinaldo, P.; Gavrilov, D.; Melan, M.; He, M.; Steinberg, S.J.; Raymond, G.V.; Vockley, J.; Gibson, K.M.
Essential fatty acid profiling for routine nutritional assessment unmasks adrenoleukodystrophy in an infant with isovaleric acidaemia
J. Inherit. Metab. Dis.
31
S453-456
2008
Homo sapiens (P26440), Homo sapiens
Bei, F.; Sun, J.H.; Yu, Y.G.; Jia, J.; Zheng, Z.J.; Fu, Q.H.; Cai, W.
Two novel isovaleryl-CoA dehydrogenase gene mutations in a Chinese infant
Gene
524
396-400
2013
Homo sapiens
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