Information on EC 1.3.8.4 - isovaleryl-CoA dehydrogenase

Word Map on EC 1.3.8.4
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
1.3.8.4
-
RECOMMENDED NAME
GeneOntology No.
isovaleryl-CoA dehydrogenase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
isovaleryl-CoA + electron-transfer flavoprotein = 3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-leucine degradation I
-
-
Metabolic pathways
-
-
Valine, leucine and isoleucine degradation
-
-
leucine metabolism
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain PAO1, gene liuA as part of the liuABCDE gene cluster
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme belongs to acyl-CoA dehydrogenase (ACD) family
malfunction
-
deficiency in isovaleryl-CoA dehydrogenase causes isovaleric acidemia, a rare inherited metabolic disease
metabolism
physiological function
additional information
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
-
-
-
?
2-methyl-hexanoyl-CoA + acceptor
2-methylhex-2-enoyl-CoA + reduced acceptor
show the reaction diagram
-
4% relative activity to isovaleryl-CoA
-
?
2-methylbutanoyl-CoA + acceptor
2-methylbut-2-enoyl-CoA + reduced acceptor
show the reaction diagram
-
low activity with the wild-type and mutant L95V/A99V/L103V/L370M/G374A
-
-
?
2-methylpalmitoyl-CoA + acceptor
2-methylhexadec-2-enoyl-CoA + reduced acceptor
show the reaction diagram
butyryl-CoA + 2,6-dichlorophenolindophenol
?
show the reaction diagram
-
high substrate specificity
-
-
?
butyryl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
show the reaction diagram
butyryl-CoA + electron-transfer flavoprotein
crotonyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
-
-
-
?
hexanoyl-CoA + acceptor
hex-2-enoyl-CoA + reduced acceptor
show the reaction diagram
hexanoyl-CoA + electron-transfer flavoprotein
hex-2-enoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
-
-
-
?
isobutyryl-CoA + acceptor
2-methylpropanoyl-CoA + reduced acceptor
show the reaction diagram
isovaleryl-CoA + 2,6-dichlorophenolindophenol
?
show the reaction diagram
-
high substrate specificity
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
show the reaction diagram
isovaleryl-CoA + electron transfer protein
3-methylcrotonoyl-CoA + reduced electron transfer protein
show the reaction diagram
-
-
-
-
?
isovaleryl-CoA + electron transfer protein
3-methylcrotonyl-CoA + reduced electron transfer protein
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
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
octanoyl-CoA + acceptor
oct-2-enoyl-CoA + reduced acceptor
show the reaction diagram
valeryl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
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
isovaleryl-CoA + 2,6-dichlorophenolindophenol
?
show the reaction diagram
-
high substrate specificity
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
show the reaction diagram
isovaleryl-CoA + electron transfer protein
3-methylcrotonoyl-CoA + reduced electron transfer protein
show the reaction diagram
-
-
-
-
?
isovaleryl-CoA + electron transfer protein
3-methylcrotonyl-CoA + reduced electron transfer protein
show the reaction diagram
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
P12007
-
-
-
?
isovaleryl-CoA + FAD
3-methylcrotonyl-CoA + FADH2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,6-dichlorophenolindophenol
-
-
electron transfer protein
-
electron transferring flavoprotein
-
-
flavin
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(Methylenecyclopropyl)acetyl-CoA
2-aza-isovaleryl-CoA
-
substrate analogue
3-methylcrotonyl-CoA
-
-
Ag+
-
completely inhibits at 0.01 mM
alpha-keto-methylenecyclopropylpropionic acid
-
-
Cu2+
-
completely inhibits at 0.01 mM
D-glucose
0.15% D-glucose represses transcription
Hg2+
-
completely inhibits at 0.1 mM
hypoglycin
iodoacetamide
-
at 2 mM 19% activity remains
L-arginine
1% L-arginine represses transcription
L-glutamate
IVD transcription is strongly repressed by L-glutamate
Methylmercury iodide
N-ethylmaleimide
p-chloromercuribenzoate
-
at 0.1 mM 18% activity remains
p-hydroxymercuribenzoate
Sucrose
-
inhibits promoter activity
valproyl-CoA
-
competitive
valproyl-dephosphoCoA
-
competitive
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Dextrin
1.15% dextrin stimulates activity
L-isoleucine
1% L-isoleucine stimulates activity
L-leucine
1% L-leucine stimulates activity
L-valine
1% L-valine stimulates activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0019 - 0.0035
(S)-2-methylbutyryl-CoA
0.025 - 0.0362
butyryl-CoA
0.0038
electron-transfer flavoprotein
-
-
0.00043
FAD
-
-
0.02 - 0.0338
Hexanoyl-CoA
0.5 - 0.79
isobutyryl-CoA
0.0013 - 0.9
isovaleryl-CoA
0.0167 - 0.4
n-valeryl-CoA
0.51 - 0.833
phenazine methosulfate
0.0105 - 0.0167
valeryl-CoA
additional information
additional information
-
kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
(S)-2-methylbutyryl-CoA
Rattus norvegicus
-
wild-type enzyme and mutant IVD G375E, pH 7.4, 37°C
0.133
butyryl-CoA
Caenorhabditis elegans
-
using recombinant enzyme, electron acceptor: electron-transferring flavoprotein
0.533
Hexanoyl-CoA
Caenorhabditis elegans
-
using recombinant enzyme, electron acceptor: electron-transferring flavoprotein
0.17 - 10
isovaleryl-CoA
0.267
valeryl-CoA
Caenorhabditis elegans
-
using recombinant enzyme, electron acceptor: electron-transferring flavoprotein
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.086 - 0.16
(S)-2-methylbutyryl-CoA
16583
0.045 - 0.53
isovaleryl-CoA
784
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
3-methylcrotonyl-CoA
-
-
0.074
valproyl-CoA
-
versus isovaleryl-CoA, pH 8.0, 37°C
0.17
valproyl-dephosphoCoA
-
versus isovaleryl-CoA, pH 8.0, 37°C
additional information
additional information
-
inhibition kinetics, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00003
-
intact mitochondria, no added acceptor
0.000039
-
mitochondria from isovaleric acidemia cells, 13% relative activity to normal cells, specific activity determined by tritium release assay
0.00016
-
sonicated mitochondria, no added acceptor
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
0.00034
-
fibroblast cell line harboring the mutation corresponding to the A282V mutant
0.00044
-
sonicated mitochondria, acceptor added: electron-transferring flavoprotein
0.00046
-
sonicated mitochondria, acceptor added: phenazine methosulfate
0.0011
-
recombinant mutant L370M/G374A, substrate 2-methylbutanoyl-CoA
0.00131
-
mitochondria from normal cells, specific activity determined by dye reduction assay
0.004
-
cell free extract of Escherichia coli cells expressing the enzyme mutant R363C
0.0041
-
normal cell lines
0.0043
-
recombinant wild-type enzyme, substrate 2-methylbutanoyl-CoA
0.005
-
sonicate
0.0062
-
purified enzyme in the absence of electron transfer agents, reaction terminated with HCl or with KMnO4/HCl
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
0.0114
-
recombinant mutant L370M/G374A, substrate butyryl-CoA
0.012
-
Triton X-100 extract
0.0125
-
sonicate supernatant fraction
0.0136
-
purified enzyme with phenazine methosulfate and dichlorophenol indophenol, reaction terminated with HCl
0.014
-
soluble extract
0.0152
-
recombinant wild-type enzyme, substrate butyryl-CoA
0.0207
-
purified enzyme with electron-transferring flavoprotein and 0.062 mM dichlorophenol indophenol, reaction terminated with HCl, concentration of isovaleryl-CoA: 0.05 mM, specific activity determined by tritium release assay
0.0239
-
recombinant mutant L370M/G374A, substrate valeryl-CoA
0.032
-
cell free extract of Escherichia coli cells expressing the enzyme mutant R382L
0.0337
-
purified enzyme, acceptor added: electron-transferring flavoprotein
0.0364
-
recombinant wild-type enzyme, substrate valeryl-CoA
0.0371
-
recombinant mutant L370M/G374A, substrate isovaleryl-CoA
0.043
-
purified enzyme, acceptor added: electron-transferring flavoprotein and 0.062 mM dichlorophenol indophenol, reaction terminated with KMnO4/HCl, concentration of isovaleryl-CoA: 0.02 mM, specific activity determined by tritium release assay; purified enzyme, acceptor added: phenazine methosulfate
0.0472
-
purified enzyme with phenazine methosulfate and dichlorophenol indophenol, reaction terminated with KMnO4/HCl
0.052
-
cell free extract of Escherichia coli cells expressing the enzyme mutant V342A
0.0572
-
purified enzyme with electron-transferring flavoprotein and 0.062 mM dichlorophenol indophenol, reaction terminated with KMnO4/HCl, concentration of isovaleryl-CoA: 0.05 mM, specific activity determined by tritium release assay
0.0754
-
recombinant wild-type enzyme, substrate isovaleryl-CoA
0.08
-
substrate: octanoyl-CoA
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
0.172
-
purified enzyme, acceptor added: electron-transferring flavoprotein and 0.062 mM dichlorophenol indophenol, concentration of isovaleryl-CoA: 0.02 mM, specific activity determined by dye reduction assay
0.3
-
partially purified enzyme, substrate: isovaleryl-CoA
0.44
-
cell free extract of Escherichia coli cells expressing the enzyme, wild type
0.51
-
butyryl-CoA as substrate and phenazine methosulfate as acceptor
0.53
-
isovaleryl-CoA as substrate and 0.0056 mM electron transfer flavoprotein as acceptor
0.6
-
of purified recombinant V342A mutant, electron acceptor: electron-transferring flavoprotein
0.64
-
hexanoyl-CoA as substrate and phenazine methosulfate as acceptor
0.72
-
isovaleryl-CoA as substrate and 0.012 mM electron transfer flavoprotein as acceptor
1
-
substrate: isovaleryl-CoA
1.09
-
valeryl-CoA as substrate and phenazine methosulfate as acceptor
1.19
-
substrate: hexanoyl-CoA
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
1.71
-
substrate: butyryl-CoA
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
2.91
-
isovaleryl-CoA as substrate and phenazine methosulfate as acceptor
3.71
-
substrate: valeryl-CoA
4.88
-
of purified recombinant R382L mutant, electron acceptor: dichlorophenol indophenol
6.34
-
of purified recombinant R382L mutant, electron acceptor: dichlorophenol indophenol + FAD
8.1
-
substrate: isovaleryl-CoA
8.2
-
of purified recombinant wild-type enzyme, electron acceptor: dichlorophenol indophenol
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
additional information
-
enzyme assay development and optimization
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
PDB
SCOP
CATH
ORGANISM
UNIPROT
Brucella suis biovar 1 (strain 1330)
Rhizobium meliloti (strain 1021)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
-
4 * 41000, recombinant LiuA, SDS-PAGE, 4 * 44000, LiuA, sequence calculation
42000
-
4 * 42000, SDS-PAGE
43098
-
4 * 43098, nucleotide sequence
44000
-
4 * 41000, recombinant LiuA, SDS-PAGE, 4 * 44000, LiuA, sequence calculation
50000
4 * 50000, about, recombinant enzyme, SDS-PAGE
75000 - 85000
-
gel filtration
87000 - 107000
-
gel filtration
146000
163000
-
recombinant enzyme, gel filtration
170000
-
gel filtration
172000
-
gel filtration
175000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
? * 43000, SDS-PAGE
tetramer
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
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48.2
-
melting point of mutant A282V without bound ligand
48.5
-
melting point of mutant A282V with isovaleryl-CoA bound
48.6
-
melting point of mutant A282V with 2-aza-isovaleryl-CoA bound
50.5
-
melting point of wild-type enzyme without bound ligand
50.9
-
melting point of wild-type enzyme with 2-aza-isovaleryl-CoA bound
55.4
-
melting point of wild-type enzyme with isovaleryl-CoA bound
additional information
-
thermal unfolding analysis
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% glycerol, 1 month
-
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
-
of recombinant enzyme, using sonication, ammonium sulfate fractionation, column chromatography on DEAE-Sepharose and hydroxyapatite
-
partially from tuber, recombinant from Escherichia coli to over 90% purity
recombinant from Escherichia coli to over 90% purity
-
recombinant LiuA from Escherichia coli
-
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 auxin affinity chromatography matrix
-
using bacterial lysates through centrifugation, filtration through an Acrodisc filter, chromatography on a XK16/20 DEAE fast-flow column and hydroxyapatite resin column
-
using chromatography on Resource Q anion exchange column, BioRad CHT2 hydroxyapatite column and phenyl ether hydrophobic interaction column
-
using DEAE-Sepharose followed by hydroxyapatite column chromatography
-
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
at the amino acid level, pea enzyme is 60% similar to human and rat enzyme
-
cDNA modified at its 5'-end coding region to enhance expression in Escherichia coli
-
clone obtained from the screening of an Arabidopsis whole plant library cDNA library
-
cloning of cDNAs of two distinct potato enzyme genes, clone obtained from the screening of a potato flower cDNA library
-
DNA and amino acid sequence determination and comparison, expression in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli
-
expression in Escherichia coli
expression in pea seedlings
-
expression of liuA in Escherichia coli strain Rosetta 2 (DE3), subcloning in Escherichia coli strain JM109
-
expression of normal and mutant enzymes in Escherichia coli
-
expression of wild-type and mutant enzyme in Escherichia coli
-
expression of wild-type and mutants in Escherichia coli
-
expression of wild-type and mutants in Escherichia coli strain JM105
-
gene ivdh, expression analysis and metabolic profiling
IVD gene, DNA and amino acid sequence deteremination and analysis, alignment of BmIVD with all 11 human acyl-CoA dehydrogenase family members, overview. Expression of wild-type BmIVD and sku-type BmIVD in Spodoptera frugiperda Sf9 cells via transfection with baculovrius
the gene spans approximately 17 kb and contains 12 coding exons organized identically to the human gene, amino acid sequences are 95.8 and 89.6% identical to that of the rat and human sequences, respectively
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
B40N
-
has no detectable enzymatic activity
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)
C328R
-
has no detectable enzymatic activity
E254D
-
has residual activity for isovaleryl-CoA, below 0.1%
E254G/A375E
-
exhibits catalytic activity toward isovaleryl-CoA
E254Q
-
has no detectable enzymatic activity
F350V
-
mutation is involved in isovaleric acidemia, no enzyme activity
G375A
-
c.1124G>A, potentially disease-associated allele
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
IVS234+85insTT
-
potentially disease-associated allele
L13P
-
has no detectable enzymatic activity
L370M/G374A
-
site-directed mutagenesis, substrate specificity similar to the wild-type enzyme, reduced activity
L383R/R387A
-
has no detectable activity in crude cellular extracts
L95V/A99V/L103V
-
site-directed mutagenesis, inactive mutant
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)
R21L
-
mutation is involved in isovaleric acidemia, no enzyme activity
R21P
-
has no detectable enzymatic activity
R382L
-
enzyme activity detected, 7% relative activity to wild-type
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
S249G
-
mutation is involved in isovaleric acidemia, no enzyme activity
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)
V342A
-
enzyme activity detected, 12% relative activity to wild-type
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
-
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
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
enzyme activity assay development for determination of isovaleric acidemia in newborn disorder screening
medicine
Show AA Sequence (915 entries)
Please use the Sequence Search for a specific query.