Information on EC 1.3.8.4 - isovaleryl-CoA dehydrogenase

Substrates: acceptors: electron-transfer flavoprotein, phenazine methosulfate
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Substrates: -
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Substrates: the catalytic activity of the recombinant wild-type enzyme is the highest in the presence of isovaleryl-CoA
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Substrates: electron acceptor: electron-transferring flavoprotein
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Substrates: electron acceptor: electron-transferring flavoprotein, dichlorophenol indophenol or dichlorophenol indophenol + FAD
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

391201, 391206, 391209

Substrates: acceptors: electron-transfer flavoprotein, phenazine methosulfate
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

391201, 391206, 391209, 391211

Substrates: -
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Substrates: -
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

391214, 391220, 655248

Substrates: -
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Substrates: -
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Substrates: isovaleryl-CoA is the preferred substrate
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Substrates: -
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Mus musculus

Q9JHI5

Substrates: -
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

391200, 391202, 391203

Substrates: isovaleryl-CoA is the preferred substrate
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

391200, 391199, 391202, 391203, 391204, 391205, 391207, 391208

Substrates: acceptors: electron-transfer flavoprotein, phenazine methosulfate
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

391199, 391203, 391204, 391205, 391207, 391208

Substrates: -
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Substrates: electron acceptor: electron-transfer flavoprotein serves as a natural electron acceptor for the enzyme with isovaleryl-CoA as substrate
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Substrates: isovaleryl-CoA is the preferred substrate
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Substrates: electron acceptor: 2,6-dichloroindophenol, intermediate electron carrier: phenazine methosulfate
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Substrates: -
Products: -

isovaleryl-CoA + electron transfer protein

3-methylcrotonoyl-CoA + reduced electron transfer protein

Substrates: -
Products: -

isovaleryl-CoA + electron transfer protein

3-methylcrotonoyl-CoA + reduced electron transfer protein

Substrates: acceptor porcine electron transfer protein
Products: -

isovaleryl-CoA + electron transfer protein

3-methylcrotonyl-CoA + reduced electron transfer protein

Substrates: -
Products: -

isovaleryl-CoA + electron transfer protein

3-methylcrotonyl-CoA + reduced electron transfer protein

Substrates: -
Products: -

isovaleryl-CoA + electron transfer protein

3-methylcrotonyl-CoA + reduced electron transfer protein

Substrates: best substrate
Products: -

isovaleryl-CoA + electron-transfer flavoprotein

3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein

Substrates: -
Products: -

isovaleryl-CoA + electron-transfer flavoprotein

3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein

Substrates: -
Products: -

isovaleryl-CoA + electron-transfer flavoprotein

3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein

Substrates: -
Products: -

isovaleryl-CoA + electron-transfer flavoprotein

3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein

Substrates: reaction via an alpha,beta-dehydrogenation step
Products: -

isovaleryl-CoA + electron-transfer flavoprotein

3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein

Substrates: -
Products: -

isovaleryl-CoA + electron-transfer flavoprotein

3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein

Substrates: -
Products: -

isovaleryl-CoA + electron-transfer flavoprotein

3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein

Substrates: -
Products: -

isovaleryl-CoA + electron-transfer flavoprotein

3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein

Substrates: -
Products: -

isovaleryl-CoA + FAD

3-methylcrotonyl-CoA + FADH2

Substrates: -
Products: -

isovaleryl-CoA + FAD

3-methylcrotonyl-CoA + FADH2

Substrates: -
Products: -

isovaleryl-CoA + FAD

3-methylcrotonyl-CoA + FADH2

Substrates: with ferrocenium hexafluorophosphate as second electron acceptor
Products: -

isovaleryl-CoA + phenazine methosulfate

3-methylcrotonyl-CoA + reduced phenazine methosulfate

655248, 391201

Substrates: -
Products: -

isovaleryl-CoA + phenazine methosulfate

3-methylcrotonyl-CoA + reduced phenazine methosulfate

Substrates: -
Products: -

n-valeryl-CoA + acceptor

pent-2-enoyl-CoA + reduced acceptor

Substrates: electron acceptor: electron-transferring flavoprotein
Products: -

n-valeryl-CoA + acceptor

pent-2-enoyl-CoA + reduced acceptor

Substrates: 46% relative specific activity to isovaleryl-CoA
Products: -

n-valeryl-CoA + acceptor

pent-2-enoyl-CoA + reduced acceptor

Substrates: -
Products: -

n-valeryl-CoA + acceptor

pent-2-enoyl-CoA + reduced acceptor

391200, 391203

Substrates: -
Products: -

n-valeryl-CoA + acceptor

pent-2-enoyl-CoA + reduced acceptor

Substrates: 32% relative specific activity to isovaleryl-CoA
Products: -

octanoyl-CoA + acceptor

oct-2-enoyl-CoA + reduced acceptor

Substrates: 7% relative activity to isovaleryl-CoA
Products: -

octanoyl-CoA + acceptor

oct-2-enoyl-CoA + reduced acceptor

Substrates: 1% relative specific activity to isovaleryl-CoA
Products: -

octanoyl-CoA + acceptor

oct-2-enoyl-CoA + reduced acceptor

Substrates: very low activity
Products: -

valeryl-CoA + acceptor

pent-2-enoyl-CoA + reduced acceptor

Substrates: -
Products: -

valeryl-CoA + acceptor

pent-2-enoyl-CoA + reduced acceptor

Substrates: low activity
Products: -

additional information

Substrates: the presence of a putative enzyme supports functional leucine catabolism in plant mitochondria
Products: -

additional information

Substrates: activity measurement using an acyl-CoA substrate and 2,6-dichloroindophenol as an electron acceptor, with phenazinemethosulfate as an intermediate electron carrier
Products: -

additional information

Substrates: activity measurement using an acyl-CoA substrate and 2,6-dichloroindophenol as an electron acceptor, with phenazinemethosulfate as an intermediate electron carrier
Products: -

additional information

Substrates: activity measurement using an acyl-CoA substrate and 2,6-dichloroindophenol as an electron acceptor, with phenazinemethosulfate as an intermediate electron carrier
Products: -

additional information

Substrates: activity measurement using an acyl-CoA substrate and 2,6-dichloroindophenol as an electron acceptor, with phenazinemethosulfate as an intermediate electron carrier
Products: -

additional information

Substrates: deficiency of the enzyme in humans is responsible for isovaleric acidemia
Products: -

additional information

Substrates: deficiency of the enzyme in humans is responsible for isovaleric acidemia
Products: -

additional information

Substrates: deficiency of the enzyme in humans is responsible for isovaleric acidemia
Products: -

additional information

Substrates: E254 of the enzyme is in close proximity to the bound FAD, E254 is the active site catalytic residue
Products: -

additional information

Substrates: E254 of the enzyme is in close proximity to the bound FAD, E254 is the active site catalytic residue
Products: -

additional information

Substrates: the location of the catalytic residue together with a glycine at position 374 is important for conferring branched-chain substrate specificity to the enzyme
Products: -

additional information

Substrates: R387 has an important role in anchoring the substrate
Products: -

additional information

Substrates: 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
Products: -

additional information

Substrates: a specific deficiency of enzyme activity is observed in cultured skin fibroblasts from patients with isovaleric acidemia
Products: -

additional information

Substrates: a specific deficiency of enzyme activity is observed in cultured skin fibroblasts from patients with isovaleric acidemia
Products: -

additional information

Substrates: the enzyme catalyzes the third step of the leucine oxidative metabolism
Products: -

additional information

Substrates: the enzyme catalyzes the third step of the leucine oxidative metabolism
Products: -

additional information

Substrates: the enzyme catalyzes the third step of the leucine oxidative metabolism
Products: -

additional information

Substrates: the enzyme catalyzes the third step of the leucine oxidative metabolism
Products: -

additional information

Substrates: the enzyme catalyzes the third step of the leucine oxidative metabolism
Products: -

additional information

Substrates: physiological implications of enzyme mutations and deficiency
Products: -

additional information

Substrates: substrate specificity of wild-type and mutant enzymes
Products: -

additional information

Substrates: isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency
Products: -

additional information

Substrates: Glu-244 is the catalytic base responsible for abstracting the alpha-proton of substrate
Products: -

additional information

Substrates: the enzyme is required in the leucine/isovalerate utilization, Liu, pathway for growth of Pseudomonas aeruginosa on acyclic terpene alcohols (citronellol) and on other methyl-branched compounds such as leucine or isovalerate, Liu proteins in metabolism of methyl-branched compounds, overview
Products: -

additional information

Substrates: no activity of LiuA with isobutyryl-CoA, 3-hydroxybutyryl-CoA, octanoyl-CoA, citronellyl-CoA or 5-methyl-hex-4-enoyl-CoA
Products: -

additional information

Substrates: the enzyme catalyzes the third step of the leucine oxidative metabolism
Products: -

additional information

Substrates: the enzyme catalyzes the dehydrogenation of monomethyl branched-chain fatty acid thioester derivatives
Products: -

additional information

Substrates: 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
Products: -

show all columns Go to Natural Substrate Search

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

isovaleryl-CoA + 2,6-dichlorophenolindophenol

Substrates: high substrate specificity
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

12 entries

isovaleryl-CoA + electron transfer protein

3-methylcrotonoyl-CoA + reduced electron transfer protein

Substrates: -
Products: -

isovaleryl-CoA + electron transfer protein

3-methylcrotonyl-CoA + reduced electron transfer protein

isovaleryl-CoA + electron-transfer flavoprotein

3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein

6 entries

isovaleryl-CoA + FAD

3-methylcrotonyl-CoA + FADH2

additional information

22 entries

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

391213, 391216, 391219

Substrates: -
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Bos taurus

391210

Substrates: -
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Substrates: -
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Substrates: -
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

391201, 391206, 391209, 391211

Substrates: -
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Substrates: -
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

391214, 391220, 655248

Substrates: -
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Substrates: -
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Mus musculus

Q9JHI5

Substrates: -
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

391199, 391203, 391204, 391205, 391207, 391208

Substrates: -
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Substrates: electron acceptor: electron-transfer flavoprotein serves as a natural electron acceptor for the enzyme with isovaleryl-CoA as substrate
Products: -

isovaleryl-CoA + acceptor

3-methylcrotonyl-CoA + reduced acceptor

Substrates: -
Products: -

isovaleryl-CoA + electron transfer protein

3-methylcrotonyl-CoA + reduced electron transfer protein

Substrates: -
Products: -

isovaleryl-CoA + electron transfer protein

3-methylcrotonyl-CoA + reduced electron transfer protein

Substrates: -
Products: -

isovaleryl-CoA + electron-transfer flavoprotein

3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein

Substrates: -
Products: -

isovaleryl-CoA + electron-transfer flavoprotein

3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein

Substrates: -
Products: -

isovaleryl-CoA + electron-transfer flavoprotein

3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein

Substrates: -
Products: -

isovaleryl-CoA + electron-transfer flavoprotein

3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein

Substrates: -
Products: -

isovaleryl-CoA + electron-transfer flavoprotein

3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein

Substrates: -
Products: -

isovaleryl-CoA + electron-transfer flavoprotein

3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein

Substrates: -
Products: -

isovaleryl-CoA + FAD

3-methylcrotonyl-CoA + FADH2

Substrates: -
Products: -

isovaleryl-CoA + FAD

3-methylcrotonyl-CoA + FADH2

Substrates: -
Products: -

additional information

Substrates: the presence of a putative enzyme supports functional leucine catabolism in plant mitochondria
Products: -

additional information

Substrates: deficiency of the enzyme in humans is responsible for isovaleric acidemia
Products: -

additional information

Substrates: deficiency of the enzyme in humans is responsible for isovaleric acidemia
Products: -

additional information

Substrates: deficiency of the enzyme in humans is responsible for isovaleric acidemia
Products: -

additional information

Substrates: E254 of the enzyme is in close proximity to the bound FAD, E254 is the active site catalytic residue
Products: -

additional information

Substrates: E254 of the enzyme is in close proximity to the bound FAD, E254 is the active site catalytic residue
Products: -

additional information

Substrates: the location of the catalytic residue together with a glycine at position 374 is important for conferring branched-chain substrate specificity to the enzyme
Products: -

additional information

Substrates: R387 has an important role in anchoring the substrate
Products: -

additional information

additional information

Substrates: a specific deficiency of enzyme activity is observed in cultured skin fibroblasts from patients with isovaleric acidemia
Products: -

additional information

Substrates: a specific deficiency of enzyme activity is observed in cultured skin fibroblasts from patients with isovaleric acidemia
Products: -

additional information

Substrates: the enzyme catalyzes the third step of the leucine oxidative metabolism
Products: -

additional information

Substrates: the enzyme catalyzes the third step of the leucine oxidative metabolism
Products: -

additional information

Substrates: the enzyme catalyzes the third step of the leucine oxidative metabolism
Products: -

additional information

Substrates: the enzyme catalyzes the third step of the leucine oxidative metabolism
Products: -

additional information

Substrates: the enzyme catalyzes the third step of the leucine oxidative metabolism
Products: -

additional information

Substrates: physiological implications of enzyme mutations and deficiency
Products: -

additional information

Substrates: isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency
Products: -

additional information

Substrates: Glu-244 is the catalytic base responsible for abstracting the alpha-proton of substrate
Products: -

additional information

additional information

Substrates: the enzyme catalyzes the third step of the leucine oxidative metabolism
Products: -

additional information

Substrates: the enzyme catalyzes the dehydrogenation of monomethyl branched-chain fatty acid thioester derivatives
Products: -

show all columns Go to Cofactor Search

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

2,6-dichlorophenolindophenol

electron transfer protein

electron transferring flavoprotein

FAD

flavin

electron transfer protein

electron transfer protein

electron transferring flavoprotein

electron transferring flavoprotein

ETF

electron transferring flavoprotein

ETF

electron transferring flavoprotein

ETF

FAD

FAD

FAD

FAD

FAD

the enzyme contains FAD as a prosthetic group, 0.6 mol FAD per mol of subunit

FAD

1 mol of FAD per subunit

FAD

FAD

flavoenzyme

FAD

show all columns Go to Inhibitor Search

FAD

FAD

FAD

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

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

391208

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

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

sucrose

inhibits promoter activity

valproyl-CoA

competitive

valproyl-dephosphoCoA

competitive

(methylenecyclopropyl)acetyl-CoA

at 0.001 mM 21% activity remains; at 0.01 mM 3% activity remains

(methylenecyclopropyl)acetyl-CoA

completely inhibits at 0.01 mM

(methylenecyclopropyl)acetyl-CoA

completely inhibits at 0.01 mM; strongly inhibits at 0.01 mM

hypoglycin

hypoglycin

inhibits, induces isovaleric acidemia when administered in experimental animals

Methylmercury iodide

Methylmercury iodide

completely inhibits at a concentration of 0.1 mM

Methylmercury iodide

N-ethylmaleimide

at 2 mM 64% activity remains

N-ethylmaleimide

completely inhibits at a concentration of 2 mM

N-ethylmaleimide

p-hydroxymercuribenzoate

p-hydroxymercuribenzoate

completely inhibits at a concentration of 0.01 mM

p-hydroxymercuribenzoate

show all columns Go to Activating Compound Search

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ACTIVATING COMPOUND

ORGANISM

UNIPROT

COMMENTARY

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

Go to Disease Search

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DISEASE

TITLE OF PUBLICATION

LINK TO PUBMED

3-hydroxyacyl-coa dehydrogenase deficiency

Epidemiology of rare diseases detected by newborn screening in the Czech Republic.

acetyl-coa c-acetyltransferase deficiency

Screening for defects of branched-chain amino acid metabolism.

acyl-coa dehydrogenase deficiency

Epidemiology of rare diseases detected by newborn screening in the Czech Republic.

acyl-coa dehydrogenase deficiency

The acyl-CoA dehydrogenation deficiencies. Recent advances in the enzymic characterization and understanding of the metabolic and pathophysiological disturbances in patients with acyl-CoA dehydrogenation deficiencies.

3892650

Adrenal Hyperplasia, Congenital

Epidemiology of rare diseases detected by newborn screening in the Czech Republic.

Biotinidase Deficiency

Epidemiology of rare diseases detected by newborn screening in the Czech Republic.

Citrullinemia

Epidemiology of rare diseases detected by newborn screening in the Czech Republic.

Congenital Hypothyroidism

Epidemiology of rare diseases detected by newborn screening in the Czech Republic.

Cystic Fibrosis

Epidemiology of rare diseases detected by newborn screening in the Czech Republic.

glutaryl-coa dehydrogenase (etf) deficiency

3892650

Homocystinuria

Epidemiology of rare diseases detected by newborn screening in the Czech Republic.

hydroxymethylglutaryl-coa lyase deficiency

Screening for defects of branched-chain amino acid metabolism.

Hyperargininemia

Epidemiology of rare diseases detected by newborn screening in the Czech Republic.

isovaleryl-coa dehydrogenase deficiency

Demonstration of a specific mitochondrial isovaleryl-CoA dehydrogenase deficiency in fibroblasts from patients with isovaleric acidemia.

6928646

isovaleryl-coa dehydrogenase deficiency

Endogenous catabolism is the major source of toxic metabolites in isovaleric acidemia.

3794887

isovaleryl-coa dehydrogenase deficiency

Epidemiology of rare diseases detected by newborn screening in the Czech Republic.

isovaleryl-coa dehydrogenase deficiency

Essential fatty acid profiling for routine nutritional assessment unmasks adrenoleukodystrophy in an infant with isovaleric acidaemia.

19089597

isovaleryl-coa dehydrogenase deficiency

Isovaleric acidemia diagnosed promptly by tandem mass spectrometry: report of one case.

15624372

isovaleryl-coa dehydrogenase deficiency

Isovaleric acidemia with promyelocytic myeloproliferative syndrome.

10191353

isovaleryl-coa dehydrogenase deficiency

L-carnitine therapy in isovaleric acidemia.

6549017

isovaleryl-coa dehydrogenase deficiency

Long Term Follow-Up of Polish Patients with Isovaleric Aciduria. Clinical and Molecular Delineation of Isovaleric Aciduria.

32977617

isovaleryl-coa dehydrogenase deficiency

Screening for defects of branched-chain amino acid metabolism.

isovaleryl-coa dehydrogenase deficiency

3892650

long-chain acyl-coa dehydrogenase deficiency

Epidemiology of rare diseases detected by newborn screening in the Czech Republic.

long-chain-3-hydroxyacyl-coa dehydrogenase deficiency

Epidemiology of rare diseases detected by newborn screening in the Czech Republic.

Maple Syrup Urine Disease

Epidemiology of rare diseases detected by newborn screening in the Czech Republic.

medium-chain acyl-coa dehydrogenase deficiency

Epidemiology of rare diseases detected by newborn screening in the Czech Republic.

Metabolic Diseases

Two novel isovaleryl-CoA dehydrogenase gene mutations in a Chinese infant.

23587913

Metabolic Diseases

[Pancytopenia and metabolic decompensation in a neonate].

27817783

Metabolic Syndrome

Broad connections in the Arabidopsis seed metabolic network revealed by metabolite profiling of an amino acid catabolism mutant.

19929878

methylcrotonoyl-coa carboxylase deficiency

Screening for defects of branched-chain amino acid metabolism.

methylenetetrahydrofolate dehydrogenase (nad+) deficiency

Epidemiology of rare diseases detected by newborn screening in the Czech Republic.

methylglutaconyl-coa hydratase deficiency

Screening for defects of branched-chain amino acid metabolism.

Muscular Diseases

Acquired multiple Acyl-CoA dehydrogenase deficiency in 10 horses with atypical myopathy.

18406615

Neoplasms

Down-regulation of metabolic proteins in hepatocellular carcinoma with portal vein thrombosis.

28785178

Riboflavin Deficiency

FAD-dependent regulation of transcription, translation, post-translational processing, and post-processing stability of various mitochondrial acyl-CoA dehydrogenases and of electron transfer flavoprotein and the site of holoenzyme formation.

1517228

Seizures

Proteomic analysis of stargazer mutant mouse neuronal proteins involved in absence seizure.

17973978

Starvation

The differential impact of amino acids on OXPHOS system activity following carbohydrate starvation in Arabidopsis cell suspensions.

28767134

Thrombosis

Down-regulation of metabolic proteins in hepatocellular carcinoma with portal vein thrombosis.

28785178

Entries 1 - 20 of 39

Show complete table

show all columns Go to KM Value Search

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.0019 - 0.0035

(S)-2-methylbutyryl-CoA

0.025 - 0.0362

butyryl-CoA

0.002

electron transfer protein

pH 8.0, 30°C, calculated per monomer

0.0038

electron-transfer flavoprotein

0.00043

FAD

0.02 - 0.0338

hexanoyl-CoA

0.5 - 0.79

isobutyryl-CoA

0.001 - 0.9

isovaleryl-CoA

36 entries

0.0167 - 0.4

n-valeryl-CoA

0.51 - 0.833

phenazine methosulfate

0.0105 - 0.0167

valeryl-CoA

additional information

kinetics

655248

0.0019

(S)-2-methylbutyryl-CoA

wild-type enzyme, pH 7.4, 37°C

0.0035

(S)-2-methylbutyryl-CoA

mutant IVD G375E, pH 7.4, 37°C

0.025

butyryl-CoA

0.0362

butyryl-CoA

0.02

hexanoyl-CoA

0.0338

hexanoyl-CoA

0.5

isobutyryl-CoA

0.79

isobutyryl-CoA

0.001

isovaleryl-CoA

pH 8.0, 30°C, calculated per monomer

0.0013

isovaleryl-CoA

per tetramer, recombinant enzyme, 32°C

0.0015

isovaleryl-CoA

wild-type

0.0023

isovaleryl-CoA

pH 7.5, 30°C, recombinant enzyme

0.0025

isovaleryl-CoA

0.0028

isovaleryl-CoA

purified enzyme V342A

0.0028

isovaleryl-CoA

purified V342A mutant, electron acceptor: electron-transferring flavoprotein

0.0029

isovaleryl-CoA

wild-type enzyme, pH 7.4, 37°C

0.0031

isovaleryl-CoA

purified wild-type enzyme, electron acceptor: electron-transferring flavoprotein

0.0031

isovaleryl-CoA

mutabt IVD E254G/G375E, pH 7.4, 37°C

0.0038

isovaleryl-CoA

mutant IVD G375E, pH 7.4, 37°C

0.0042

isovaleryl-CoA

purified enzyme

0.0045

isovaleryl-CoA

purified R382L mutant, electron acceptor: dichlorophenol indophenol

0.006

isovaleryl-CoA

partially purified enzyme

0.0063

isovaleryl-CoA

sonic supernatant

0.0069

isovaleryl-CoA

purified R382L mutant, electron acceptor: electron-transferring flavoprotein

0.0113

isovaleryl-CoA

0.0113

isovaleryl-CoA

purified enzyme in the absence of electron transfer agents

0.013

isovaleryl-CoA

whole sonicate

0.0132

isovaleryl-CoA

0.0132

isovaleryl-CoA

purified enzyme with electron-transferring flavoprotein and dichlorophenol indophenol, reaction terminated with KMnO4/HCl

0.014

isovaleryl-CoA

0.0203

isovaleryl-CoA

mutant R387K

0.0208

isovaleryl-CoA

0.0208

isovaleryl-CoA

purified enzyme with phenazine methosulfate and dichlorophenol indophenol, reaction terminated with KMnO4/HCl

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

0.033

isovaleryl-CoA

with phenazine methosulfate as an artificial electron acceptor

0.047

isovaleryl-CoA

0.05

isovaleryl-CoA

0.0756

isovaleryl-CoA

mutant R387A

0.125

isovaleryl-CoA

pH 8.0, 37°C

0.195

isovaleryl-CoA

mutant R387Q

0.41

isovaleryl-CoA

purified A282V mutant, electron acceptor: dichlorophenol indophenol

0.9

isovaleryl-CoA

mutant R387E

0.0167 - 0.4

n-valeryl-CoA

0.0167 - 0.4

n-valeryl-CoA

0.0748

n-valeryl-CoA

partially purified enzyme

0.4

n-valeryl-CoA

0.51

phenazine methosulfate

0.833

phenazine methosulfate

0.0105

valeryl-CoA

0.0167

valeryl-CoA

show all columns Go to Turnover Number Search

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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

0.133

butyryl-CoA

using recombinant enzyme, electron acceptor: electron-transferring flavoprotein

0.533

hexanoyl-CoA

using recombinant enzyme, electron acceptor: electron-transferring flavoprotein

0.17 - 10

isovaleryl-CoA

13 entries

0.267

valeryl-CoA

using recombinant enzyme, electron acceptor: electron-transferring flavoprotein

0.17

isovaleryl-CoA

mutant IVD G375E, pH 7.4, 37°C

0.283

isovaleryl-CoA

purified V342A mutant, electron acceptor: dichlorophenol indophenol

0.32

isovaleryl-CoA

mutabt IVD E254G/G375E, pH 7.4, 37°C

0.733

isovaleryl-CoA

purified R382L mutant, electron acceptor: dichlorophenol indophenol

0.817

isovaleryl-CoA

purified V342A mutant, electron acceptor: electron-transferring flavoprotein

0.98

isovaleryl-CoA

per tetramer, recombinant enzyme, 32°C

1.5

isovaleryl-CoA

wild-type enzyme, pH 7.4, 37°C

isovaleryl-CoA

purified R382L mutant, electron acceptor: electron-transferring flavoprotein

2.2

isovaleryl-CoA

purified A282V mutant, electron acceptor: electron-transferring flavoprotein

2.37

isovaleryl-CoA

using recombinant enzyme, 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

isovaleryl-CoA

purified wild-type enzyme, electron acceptor: dichlorophenol indophenol

show all columns Go to kcat/KM Value Search

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kcat/KM VALUE [1/mMs^-1]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.086 - 0.16

(S)-2-methylbutyryl-CoA

0.045 - 4300

isovaleryl-CoA

0.086

(S)-2-methylbutyryl-CoA

mutant IVD G375E, pH 7.4, 37°C

0.16

(S)-2-methylbutyryl-CoA

wild-type enzyme, pH 7.4, 37°C

0.045

isovaleryl-CoA

mutant IVD G375E, pH 7.4, 37°C

0.1

isovaleryl-CoA

mutabt IVD E254G/G375E, pH 7.4, 37°C

0.53

isovaleryl-CoA

wild-type enzyme, pH 7.4, 37°C

4300

isovaleryl-CoA

pH 8.0, 30°C, calculated per monomer

show all columns Go to Ki Value Search

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Ki VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.02

3-methylcrotonyl-CoA

1.5

RYATLPNIMKAK

pH 8.0, 30°C

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

inhibition kinetics, overview

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

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

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

391207

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

0.03

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

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

0.086

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

0.832

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

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

2.68

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

additional information

enzyme assay development and optimization

0.0041

normal cell lines

0.0041

normal cell lines

0.03

butyryl-CoA as substrate and 0.0056 mM electron transfer flavoprotein as acceptor

0.03

partially purified enzyme, substrate: n-valeryl-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

0.043

purified enzyme, acceptor added: phenazine methosulfate

0.086

cell free extract of Escherichia coli cells expressing the enzyme mutant A282V

0.086

0.086

substrate: n-butyryl-CoA

0.832

0.832

substrate: n-valeryl-CoA

2.68

2.68

substrate: isovaleryl-CoA

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

7.4

assay at

7.5

7.5

assay at

7.5

assay at

7.5

assay at

assay at

isovaleryl-CoA + phenazine methosulfate

show all columns Go to Temperature Optimum Search

isovaleryl-CoA + phenazine methosulfate

assay at

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

assay at

assay at

show all columns Go to Organism Search

assay at

assay at

assay at

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

gene ivdh

UniProt

brenda

Arabidopsis thaliana Landsberg erecta

UniProt

brenda

gene atIVD

UniProt

brenda

UniProt

brenda

UniProt

brenda

UniProt

brenda

UniProt

brenda

Bos taurus

391210

brenda

brenda

brenda

Halobacterium salinarum NRC34001

711521, 762821

brenda

brenda

brenda

Uniprot

brenda

UniProt

brenda

UniProt

brenda

gene liuA as part of the liuABCDE gene cluster

brenda

391213, 391216, 391219

brenda

UniProt

brenda

gene atIVD

UniProt

brenda

gene ivdh

UniProt

brenda

391201, 391206, 391209, 391211

brenda

Swissprot

brenda

391214, 391220, 654890, 655248, 656288

brenda

689020, 699381

Swissprot

brenda

brenda

Swissprot

brenda

expressed in Escherichia coli

676020

brenda

genetic mutation profile of isovaleric acidemia patients in Taiwan

brenda

391199, 391200, 391202, 391203, 391204, 391205, 391207, 391208

brenda

724512, 724826

UniProt

brenda

isozyme IVD2

SwissProt

brenda

potato

brenda

show all columns Go to Source Tissue Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

brenda

brenda

peripheral

brenda

genetic mutation profile of isovaleric acidemia patients in Taiwan

brenda

brenda

brenda

brenda

brenda

brenda

brenda

mature

brenda

brenda

leaf

Arabidopsis thaliana Landsberg erecta

mature

brenda

brenda

brenda

brenda

391199, 391200, 391202, 391203, 391204, 391205, 391207, 391208

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

show all columns Go to Localization Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

brenda

brenda

391213, 391216, 391219

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

391199, 391200, 391202, 391203, 391204, 391205, 391207, 391208

brenda

brenda

brenda

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

show all columns Go to General Information Search

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

evolution

malfunction

metabolism

8 entries

physiological function

additional information

13 entries

evolution

the enzyme belongs to acyl-CoA dehydrogenase (ACD) family

evolution

isovaleryl-CoA dehydrogenase (and its corresponding gene) is widely distributed in mammals, plants, and bacteria. This enzyme belongs to the acyl-CoA dehydrogenase family, which are responsible for hydrogen transfer in flavoproteins

malfunction

deficiency in isovaleryl-CoA dehydrogenase causes isovaleric acidemia, a rare inherited metabolic disease

malfunction

during sugar starvation arising from the exposure of wild-type plants to darkness, autophagic transport of chloroplast stroma, which contains most of the proteins in a leaf, into the vacuolar lumen is induced within 2 days. During this time, the level of soluble proteins, primarily Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase), decreases and the amount of free amino acid increases. In dark-treated autophagy-defective (atg) mutants, the decrease of soluble proteins is suppressed, which results in the compromised release of basic amino acids, branched-chain amino acids (BCAAs) and aromatic amino acids. The impairment of BCAA catabolic pathways in the knockout mutants of the electron transfer flavoprotein (ETF)/ETF:ubiquinone oxidoreductase (etfqo) complex and the electron donor protein isovaleryl-CoA dehydrogenase (ivdh) cause a reduced tolerance to dark treatment similar to that in the atg mutants. The enhanced accumulation of BCAAs in the ivdh and etfqo mutants during the dark treatment is reduced by additional autophagy deficiency. These results indicate that vacuolar protein degradation via autophagy serves as an adaptive response to disrupted photosynthesis by providing substrates to amino acid catabolic pathways, including BCAA catabolism mediated by IVDH and ETFQO. Knockout mutants atg10-1, atg5-1, and atg2-1, phenotypes, overview

malfunction

metabolism

IVD acts in the third step of leucine degradation

metabolism

isovaleryl-CoA dehydrogenase is an important enzyme in branched chain amino acid metabolism. The pathway of leucine to mevalonate in halophilic archaea involves efficient incorporation of leucine into isoprenoidal lipid with the requirement of isovaleryl-CoA dehydrogenase in Halobacterium salinarum, overview

711521

metabolism

involvement of isovaleryl-CoA dehydrogenase in leucine conversion to isoprenoid lipid in halophilic archaea, involvement of the leucine-to-mevalonate pathway, especially isovaleryl-CoA dehydrogenase, in the production of 3-methylcrotonyl-CoA. Branched amino acids are metabolized to mevalonate in archaea in a manner similar to other organisms, metabolic pathway overview

metabolism

BCAA transaminase 2 (BCAT2) and the branched-chain alpha2-oxo acid dehydrogenase complex subunit E1A1 (BCKDH E1A1) are involved in BCAA catabolism by providing substrates to enzyme IVDH. During sugar starvation arising from the exposure of wild-type plants to darkness, autophagic transport of chloroplast stroma, which contains most of the proteins in a leaf, into the vacuolar lumen is induced within 2 days. During this time, the level of soluble proteins, primarily Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase), decreases and the amount of free amino acid increases. Vacuolar protein degradation via autophagy serves as an adaptive response to disrupted photosynthesis by providing substrates to amino acid catabolic pathways, including BCAA catabolism mediated by IVDH and ETFQO, involving the isovaleryl-CoA dehydrogenase (ivdh). Autophagy and amino acid catabolism are important in the plant response to sugar starvation. Relationship between autophagy and amino acid catabolism via the ETF/ETFQO system, overview

metabolism

metabolism

IVD acts in the third step of leucine degradation

metabolism

Halobacterium salinarum NRC34001

IVD acts in the third step of leucine degradation

metabolism

physiological function

IVD catalyzes the stereospecific conversion of the diastereotopic methyl group of leucine to isoprenoidal lipids

711521

physiological function

involvement of ivdh in phytol degradation during dark-Induced starvation

Halobacterium salinarum NRC34001

physiological function

IVD catalyzes the stereospecific conversion of the diastereotopic methyl group of leucine to isoprenoidal lipids

physiological function

involvement of ivdh in phytol degradation during dark-Induced starvation

additional information

a G376V molecular defect of isovaleryl-CoA dehydrogenase, IVD, causes IVD deficiency which is responsible for the isovaleric acid-emanating skunk mutant odorous phenotype with prepupal lethality of the silkworm, molecular modelling, overview. The sku larvae begins emanating isovaleric acid odour from the first day after hatching, but does not show any signs of developmental abnormality until the onset of spinning. The mutants start spinning after the normal duration of the final instar, 6-8 days, but stop after a short time and develop a very thin cocoon. They eventually die without becoming pupae in about a week after spinning

additional information

additional information

impaired branched chain amino acid catabolic enzyme isovaleryl-CoA dehydrogenase causes a metabolic syndrome with increased seed homomethionine and isovaleroyloxypropyl-glucosinolate, along with reduced 3-benzoyloxypropyl-glucosinolate, a diverse set of metabolites is affected in the ivd1 mutants, complementary metabolite profiling analysis, overview

additional information

additional information

responses of Arabidopsis thaliana mutants deficient in the expression of isovaleryl-CoA dehydrogenase and 2-hydroxyglutarate dehydrogenase to extended darkness and other environmental stresses, phenotype, overview. Isovaleryl-CoA dehydrogenase is the more critical for alternative respiration. Both isovaleryl-CoA dehydrogenase and 2-hydroxyglutarate dehydrogenase act as electron donors to the ubiquinol pool via an electron-transfer flavoprotein/electron-transfer flavoprotein:ubiquinone oxidoreductase-mediated route

additional information

additional information

the enzyme reactions stereochemical course is anti-elimination

additional information

residue E246 is the predicted active site catalytic residue of the enzyme

additional information

residue E246 is the predicted active site catalytic residue of the enzyme

additional information

additional information

Arabidopsis thaliana Landsberg erecta

additional information

additional information

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

Show AA Sequence and Transmembrane Helices (6499 entries)
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Go to PDB and Structure Links Search

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PDB

SCOP

CATH

UNIPROT

ORGANISM

show all columns Go to Molecular Weight Search

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

146000

163000

recombinant enzyme, gel filtration

170000

gel filtration

172000

gel filtration

175000

gel filtration

41000

4 * 41000, recombinant LiuA, SDS-PAGE, 4 * 44000, LiuA, sequence calculation

42000

4 * 42000, SDS-PAGE

43000

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

recombinant enzyme, gel filtration

146000

recombinant enzyme, gel filtration

43000

4 * 43000, SDS-PAGE

43000

show all columns Go to Subunit Search

4 * 43000, SDS-PAGE

43000

? * 43000, SDS-PAGE

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

? * 43000, SDS-PAGE

tetramer

6 entries

tetramer

4 * 43000, SDS-PAGE

tetramer

4 * 42000, SDS-PAGE

tetramer

4 * 41000, recombinant LiuA, SDS-PAGE, 4 * 44000, LiuA, sequence calculation

tetramer

4 * 43000, SDS-PAGE

tetramer

4 * 43098, nucleotide sequence

tetramer

4 * 50000, about, recombinant enzyme, SDS-PAGE

Go to Crystallization (commentary) Search

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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

show all columns Go to Protein Variants Search

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

G376V

A282V

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

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

I199M

naturally occuring missense mutation in a Chinese infant, G39A genotype, phenotype, overview

IVS234+85insTT

potentially disease-associated allele

699381

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

R21L

mutation is involved in isovaleric acidemia, no enzyme activity

R21P

has no detectable enzymatic activity

R363C

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

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

Y166F

mutation does not block enzyme interaction with the electron transfer protein

Y371C

E246Q

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

7 entries

G376V

the mutation has negative effects on FAD-binding or on monomer-monomer interactions of the skunk mutant enzyme, like in strain a85, the mutant shows a odorous phenotype with prepupal lethality

G376V

the mutation has negative effects on FAD-binding or on monomer-monomer interactions of the skunk mutant enzyme, like in strain a85, the mutant shows a odorous phenotype with prepupal lethality

G376V

the mutation has negative effects on FAD-binding or on monomer-monomer interactions of the skunk mutant enzyme, like in strain a85, the mutant shows a odorous phenotype with prepupal lethality

A282V

enzyme activity detected, 19% relative activity to wild-type

A282V

site-directed mutagenesis, severely affected interaction between enzyme and flavin cofactor, about 40% reduced activity compared to the wild-type enzyme

E254G

has no detectable enzymatic activity

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

676020

R363C

enzyme activity detected, 1% relative activity to wild-type

R363C

E246Q

site-directed mutagenesis, the recombinant IVDH enzyme mutant is obtained as an apoprotein, the protein is fully reconstituted by incubation with flavin adenine dinucleotide (FAD) at a ratio 1:20 (IVDH: FAD) molar excess. The reconstituted E246Q IVDH has no activity for isovaleryl-CoA. The mutant IVDH is unable to form charge transfer complex as a result of altering catalytic residue E246

E246Q

additional information

construction of T-DNA mutant line GK756G02, an enzyme-deficient mutant with full-length ORFs including stop codons of IVDH, phenotype, overview

additional information

construction of T-DNA mutant line GK756G02, an enzyme-deficient mutant with full-length ORFs including stop codons of IVDH, phenotype, overview

additional information

knockout mutants atg10-1, atg5-1, and atg2-1, as well as ivdh-1 and etfqo-1 mutants, phenotypes, overview. Dark-induced increases in specific amino acid levels are compromised in atg mutants. Comparison of the amino acid levels between ivdh-1 or etfqo-1 mutants and the wild-type shows that total amino acid levels increase similarly after the dark treatment among those plants, mainly caused by increases in the BCAAs, basic amino acids, aromatic amino acids and Asn. The dark-induced increase of Glu is suppressed in ivdh-1 and etfqo-1. Among the individual amino acids that do not increase in the dark-treated wild-type, the decrease in alanine levels is exacerbated in both ivdh-1 and etfqo-1. These results show the attenuation of BCAA catabolism in the mutants. The accumulation of BCAAs after 2 days of dark treatment is enhanced in ivdh-1 and etfqo-1 compared with to wild-type supporting the suggestion that BCAAs are catabolized via IVDH and the ETF/ETFQO system from an early period of dark treatment. The ivdh-1 and etfqo-1 mutations do not affect the dark-induced increases in the levels of basic amino acids (Lys, Arg, and His) and aromatic amino acids (Phe, Tyr, and Trp) compared with to wild-type plants

additional information

additional information

construction of T-DNA mutant line GK756G02, an enzyme-deficient mutant with full-length ORFs including stop codons of IVDH, phenotype, overview

additional information

additional information

construction of insertion mutants, which show completely impaired growth on all acyclic terpenes tested, i.e.citronellol, geraniol, sodium salts of citronellate and geranylate, and on leucine and isovalerate, phenotype, overview

show all columns Go to Temperature Stability Search

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

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

Go to Storage Stability Search

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STORAGE STABILITY

ORGANISM

UNIPROT

LITERATURE

-20°C, 50% glycerol, 1 month

Go to Purification (commentary) Search

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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

recombinant Strep-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by affinity 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 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

391205

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

Go to Cloned (commentary) Search

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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

gene Pden_3633, located on chromosome 2, recombinant expression of Strep-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)

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

Mus musculus

Q9JHI5

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

expression in Escherichia coli

expression in Escherichia coli

expression in Escherichia coli

expression of normal and mutant enzymes in Escherichia coli

expression of normal and mutant enzymes in Escherichia coli

Go to Expression Search

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EXPRESSION

ORGANISM

UNIPROT

LITERATURE

transcript levels of BCAT2, BCKDH E1A1, IVDH and ETFQO are increased after the 2 days dark treatment in both the wild-type and the atg5-1 mutant

transcript levels of BCAT2, BCKDH E1A1, IVDH and ETFQO are increased after the 2 days dark treatment in both the wild-type and the atg5-1 mutant

transcript levels of BCAT2, BCKDH E1A1, IVDH and ETFQO are increased after the 2 days dark treatment in both the wild-type and the atg5-1 mutant

Go to Renatured Search

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RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

the recombinant IVDH enzyme mutant E246Q is obtained as an apoprotein, the protein is fully reconstituted to the holoprotein by incubation with flavin adenine dinucleotide (FAD) at a ratio 1:20 (IVDH: FAD) molar excess. The reconstituted E246Q IVDH has no activity for isovaleryl-CoA

show all columns Go to Application Search

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

diagnostics

enzyme activity assay development for determination of isovaleric acidemia in newborn disorder screening

medicine

medicine

isovaleric acidemia is caused by isovaleryl-CoA dehydrogenase deficiency

medicine

top print hide References Search

isovaleric acidaemia, caused by isovaleryl coenzyme A dehydrogenase deficiency, is an autosomal-recessive disorder of L-leucine catabolism

699381

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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

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264

16321-16331

1989

Rattus norvegicus

2777793

brenda

Ikeda, Y.; Tanaka, K.

Isovaleryl-CoA dehydrogenase from rat liver

Methods Enzymol.

166

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1988

Rattus norvegicus

2853821

brenda

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

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7982-7989

1987

Homo sapiens

3597357

brenda

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

6401713

brenda

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.

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1983

Rattus norvegicus

6401712

brenda

Rhead, W.J.; Hall, C.; Tanaka, K.

Novel tritium release assays for isovaleryl-CoA and butyryl-CoA dehydrogenases

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256

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1981

Rattus norvegicus, Cavia porcellus

7007368

brenda

391205

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

2646-2650

1980

Rattus norvegicus

6930657

brenda

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

580-583

1980

Homo sapiens

6928646

brenda

391207

Osmundsen, H.; Billington, D.; Sherrat, H.S.A.

Evidence for a separate isovaleryl-coenzyme A dehydrogenase in liver mitochondria

Biochem. Soc. Trans.

1286-1288

1974

Rattus norvegicus

brenda

391208

Tanaka, K.; Miller, E.M.; Isselbacher, K.J.

Hypoglycin A: a specific inhibitor of isovaleryl CoA dehydrogenase

Proc. Natl. Acad. Sci. USA

20-24

1971

Rattus norvegicus

5276292

brenda

Mohsen, A.W.A.; Vockley, J.

Identification of the active site catalytic residue in human isovaleryl-CoA dehydrogenase

Biochemistry

10146-10152

1995

Homo sapiens

7640268

brenda

391210

Hazekawa, I.; Nishina, Y.; Sato, K.; Shichiri, M.; Shiga, K.

Substrate activating mechanism of short-chain acyl-CoA, medium-chain acyl-CoA, long-chain acyl-CoA, and isovaleryl-CoA dehydrogenases from bovine liver: a resonance Raman study on the 3-ketoacyl-CoA complexes

J. Biochem.

118

900-910

1995

Bos taurus

8749305

brenda

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

8455-8464

1997

Homo sapiens

9214289

brenda

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

10325-10335

1998

Homo sapiens (P26440), Homo sapiens

9665741

brenda

Daschner, K.; Thalheim, C.; Guha, C.; Brennicke, A.; Binder, S.

In plants a putative isovaleryl-CoA-dehydrogenase is located in mitochondria

Plant Mol. Biol.

1275-1282

1999

Arabidopsis thaliana

10380813

brenda

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

10713113

brenda

Reinard, T.; Janke, V.; Willard, J.; Buck, F.; Jacobsen, H.J.; Vockley, J.

Cloning of a gene for an acyl-CoA dehydrogenase from Pisum sativum L. and purification and characterization of its product as an isovaleryl-CoA dehydrogenase

J. Biol. Chem.

275

33738-33743

2000

Lathyrus oleraceus

10913142

brenda

Faivre-Nitschke, S.E.; Couee, I.; Vermel, M.; Grienenberger, J.M.; Gualberto, J.M.

Purification, characterization and cloning of isovaleryl-CoA dehydrogenase from higher plant mitochondria

Eur. J. Biochem.

268

1332-1339

2001

Arabidopsis thaliana, Solanum tuberosum

11231285

brenda

Willard, J.M.; Reinard, T.; Mohsen, A.W.; Vockley, J.

Cloning of genomic and cDNA for mouse isovaleryl-CoA dehydrogenase (IVD) and evolutionary comparison to other known IVDs

Gene

270

253-257

2001

Mus musculus (Q9JHI5), Mus musculus

11404023

brenda

Mohsen, A.W.A.; Navarette, B.; Vockley, J.

Identification of Caenorhabditis elegans isovaleryl-CoA dehydrogenase and structural comparison with other scyl-CoA dehydrogenases

Mol. Genet. Metab.

126-137

2001

Caenorhabditis elegans

11386848

brenda

Daschner, K.; Couee, I.; Binder, S.

The mitochondrial isovaleryl-coenzyme A dehydrogenase of Arabidopsis oxidizes intermediates of leucine and valine catabolism

Plant Physiol.

126

601-612

2001

Arabidopsis thaliana

11402190

brenda

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.

226-237

2001

Homo sapiens

11592819

brenda

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

15337167

brenda

655248

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

15698607

brenda

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

15574432

brenda

676020

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.

232-242

2006

Homo sapiens

brenda

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.

134-139

2007

Homo sapiens

17027310

brenda

Yamashita, N.; Sakamoto, K.; Yamada, O.; Akita, O.; Nishimura, A.

The promoter activity of isovaleryl-CoA dehydrogenase-encoding gene (ivdA) from Aspergillus oryzae is strictly repressed by glutamic acid

Biosci. Biotechnol. Biochem.

1561-1563

2007

Aspergillus oryzae (Q75N94), Aspergillus oryzae

17587691

brenda

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.

71-77

2007

Homo sapiens (P26440), Homo sapiens

17576084

brenda

Foerster-Fromme, K.; Jendrossek, D.

Biochemical characterization of isovaleryl-CoA dehydrogenase (LiuA) of Pseudomonas aeruginosa and the importance of liu genes for a functional catabolic pathway of methyl-branched compounds

FEMS Microbiol. Lett.

286

78-84

2008

Pseudomonas aeruginosa

18625020

brenda

699381

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.

S453-456

2008

Homo sapiens (P26440), Homo sapiens

19089597

brenda

711521

Yamauchi, N.

The pathway of leucine to mevalonate in halophilic archaea: efficient incorporation of leucine into isoprenoidal lipid with the involvement of isovaleryl-CoA dehydrogenase in Halobacterium salinarum

Biosci. Biotechnol. Biochem.

443-446

2010

Halobacterium salinarum, Halobacterium salinarum NRC34001

20139592

brenda

Urano, K.; Daimon, T.; Banno, Y.; Mita, K.; Terada, T.; Shimizu, K.; Katsuma, S.; Shimada, T.

Molecular defect of isovaleryl-CoA dehydrogenase in the skunk mutant of silkworm, Bombyx mori

FEBS J.

277

4452-4463

2010

Bombyx mori (B5UB85), Bombyx mori, Bombyx mori c108T (B5UB85), Bombyx mori p50T (B5UB85)

21040472

brenda

Araujo, W.L.; Ishizaki, K.; Nunes-Nesi, A.; Larson, T.R.; Tohge, T.; Krahnert, I.; Witt, S.; Obata, T.; Schauer, N.; Graham, I.A.; Leaver, C.J.; Fernie, A.R.

Identification of the 2-hydroxyglutarate and isovaleryl-CoA dehydrogenases as alternative electron donors linking lysine catabolism to the electron transport chain of Arabidopsis mitochondria

Plant Cell

1549-1563

2010

Arabidopsis thaliana (Q9SWG0), Arabidopsis thaliana, Arabidopsis thaliana Col ecotype (Q9SWG0)

20501910

brenda

Gu, L.; Jones, A.D.; Last, R.L.

Broad connections in the Arabidopsis seed metabolic network revealed by metabolite profiling of an amino acid catabolism mutant

Plant J.

579-590

2010

Arabidopsis thaliana (Q9SWG0), Arabidopsis thaliana, Arabidopsis thaliana Landsberg erecta (Q9SWG0)

19929878

brenda

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.

1-8

2013

Rattus norvegicus (P12007)

23474214

brenda

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.

1155-1160

2011

Rattus norvegicus (P12007)

21430231

brenda

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

23587913

brenda

Mohsen, A.W.; Vockley, J.

Kinetic and spectral properties of isovaleryl-CoA dehydrogenase and interaction with ligands

Biochimie

108

108-119

2015

Homo sapiens (P26440), Homo sapiens

25450250

brenda

Yamauchi, N.; Tanoue, R.

Deuterium incorporation experiments from (3R)- and (3S)-[3-2H]leucine into characteristic isoprenoidal lipid-core of halophilic archaea suggests the involvement of isovaleryl-CoA dehydrogenase

Biosci. Biotechnol. Biochem.

2062-2070

2017

Halobacterium salinarum

28942710

brenda

Karim, R.M.

Identification of isovaleryl-CoA dehydrogenase catalytic residue in Paracoccus denitrificans PD1222

Plant Arch.

3091-3096

2020

Paracoccus denitrificans (A1B856), Paracoccus denitrificans Pd1222 (A1B856)

brenda