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(S)-2-methylbutyryl-CoA + electron-transfer flavoprotein
2-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
2-methyl-hexanoyl-CoA + acceptor
2-methylhex-2-enoyl-CoA + reduced acceptor
-
4% relative activity to isovaleryl-CoA
-
?
2-methylbutanoyl-CoA + acceptor
2-methylbut-2-enoyl-CoA + reduced acceptor
-
low activity with the wild-type and mutant L95V/A99V/L103V/L370M/G374A
-
-
?
2-methylpalmitoyl-CoA + acceptor
2-methylhexadec-2-enoyl-CoA + reduced acceptor
butyryl-CoA + 2,6-dichlorophenolindophenol
?
-
high substrate specificity
-
-
?
butyryl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
butyryl-CoA + electron-transfer flavoprotein
crotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
hexanoyl-CoA + acceptor
hex-2-enoyl-CoA + reduced acceptor
hexanoyl-CoA + electron-transfer flavoprotein
hex-2-enoyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
isobutyryl-CoA + acceptor
2-methylpropanoyl-CoA + reduced acceptor
isovaleryl-CoA + 2,6-dichlorophenolindophenol
?
-
high substrate specificity
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
isovaleryl-CoA + electron transfer protein
3-methylcrotonoyl-CoA + reduced electron transfer protein
isovaleryl-CoA + electron transfer protein
3-methylcrotonyl-CoA + reduced electron transfer protein
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
isovaleryl-CoA + FAD
3-methylcrotonyl-CoA + FADH2
isovaleryl-CoA + phenazine methosulfate
3-methylcrotonyl-CoA + reduced phenazine methosulfate
n-valeryl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
octanoyl-CoA + acceptor
oct-2-enoyl-CoA + reduced acceptor
valeryl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
additional information
?
-
2-methylpalmitoyl-CoA + acceptor
2-methylhexadec-2-enoyl-CoA + reduced acceptor
-
7% relative activity to isovaleryl-CoA
-
?
2-methylpalmitoyl-CoA + acceptor
2-methylhexadec-2-enoyl-CoA + reduced acceptor
-
minor activity
-
?
2-methylpalmitoyl-CoA + acceptor
2-methylhexadec-2-enoyl-CoA + reduced acceptor
-
minor activity
-
?
2-methylpalmitoyl-CoA + acceptor
2-methylhexadec-2-enoyl-CoA + reduced acceptor
-
minor activity
-
?
butyryl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
-
electron acceptor: electron-transferring flavoprotein
-
?
butyryl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
-
-
-
-
?
butyryl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
-
acceptor: phenazine methosulfate
-
?
butyryl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
-
21% relative specific activity to isovaleryl-CoA
-
?
butyryl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
-
3.3% relative activity to isovaleryl-CoA
-
?
butyryl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
low activity
-
-
?
hexanoyl-CoA + acceptor
hex-2-enoyl-CoA + reduced acceptor
-
weak activity
-
?
hexanoyl-CoA + acceptor
hex-2-enoyl-CoA + reduced acceptor
-
electron acceptor: electron-transferring flavoprotein
-
?
hexanoyl-CoA + acceptor
hex-2-enoyl-CoA + reduced acceptor
-
acceptor: phenazine methosulfate
-
?
hexanoyl-CoA + acceptor
hex-2-enoyl-CoA + reduced acceptor
-
15% relative specific activity to isovaleryl-CoA
-
?
hexanoyl-CoA + acceptor
hex-2-enoyl-CoA + reduced acceptor
low activity
-
-
?
isobutyryl-CoA + acceptor
2-methylpropanoyl-CoA + reduced acceptor
-
20% relative activity to isovaleryl-CoA
-
?
isobutyryl-CoA + acceptor
2-methylpropanoyl-CoA + reduced acceptor
-
the activity with isobutyryl-CoA implies an additional role of the enzyme in the catabolism of valine
-
?
isobutyryl-CoA + acceptor
2-methylpropanoyl-CoA + reduced acceptor
-
the activity with isobutyryl-CoA implies an additional role of the enzyme in the catabolism of valine
-
?
isobutyryl-CoA + acceptor
2-methylpropanoyl-CoA + reduced acceptor
-
the activity with isobutyryl-CoA implies an additional role of the enzyme in the catabolism of valine
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
isovaleryl-CoA is the preferred substrate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
isovaleryl-CoA is the preferred substrate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
electron acceptor: ferricenium hexafluorophosphate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
isovaleryl-CoA is the preferred substrate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
electron acceptor: electron-transferring flavoprotein
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
enzyme activity observed in the absence of electron transfer agents suggests that rapid tritium exchange occurs between the enzyme-bound substrate and the incubation medium
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
the catalytic activity of the recombinant wild-type enzyme is the highest in the presence of isovaleryl-CoA
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
electron acceptor: electron-transferring flavoprotein
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
electron acceptor: electron-transferring flavoprotein, dichlorophenol indophenol or dichlorophenol indophenol + FAD
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
isovaleryl-CoA is the preferred substrate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
isovaleryl-CoA is the preferred substrate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
isovaleryl-CoA is the preferred substrate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
isovaleryl-CoA is the preferred substrate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
acceptors: electron-transfer flavoprotein, phenazine methosulfate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
electron acceptor: electron-transfer flavoprotein serves as a natural electron acceptor for the enzyme with isovaleryl-CoA as substrate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
electron acceptor: electron-transfer flavoprotein serves as a natural electron acceptor for the enzyme with isovaleryl-CoA as substrate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
isovaleryl-CoA is the preferred substrate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
electron acceptor: 2,6-dichloroindophenol, intermediate electron carrier: phenazine methosulfate
-
?
isovaleryl-CoA + electron transfer protein
3-methylcrotonoyl-CoA + reduced electron transfer protein
-
-
-
-
?
isovaleryl-CoA + electron transfer protein
3-methylcrotonoyl-CoA + reduced electron transfer protein
acceptor porcine electron transfer protein
-
-
?
isovaleryl-CoA + electron transfer protein
3-methylcrotonyl-CoA + reduced electron transfer protein
-
-
-
-
?
isovaleryl-CoA + electron transfer protein
3-methylcrotonyl-CoA + reduced electron transfer protein
-
-
-
?
isovaleryl-CoA + electron transfer protein
3-methylcrotonyl-CoA + reduced electron transfer protein
best substrate
-
-
?
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
-
?
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
reaction via an alpha,beta-dehydrogenation step
-
-
?
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
-
r
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
isovaleryl-CoA + FAD
3-methylcrotonyl-CoA + FADH2
-
-
-
-
?
isovaleryl-CoA + FAD
3-methylcrotonyl-CoA + FADH2
-
-
-
?
isovaleryl-CoA + FAD
3-methylcrotonyl-CoA + FADH2
with ferrocenium hexafluorophosphate as second electron acceptor
-
-
?
isovaleryl-CoA + phenazine methosulfate
3-methylcrotonyl-CoA + reduced phenazine methosulfate
-
-
-
-
?
isovaleryl-CoA + phenazine methosulfate
3-methylcrotonyl-CoA + reduced phenazine methosulfate
-
-
-
-
?
n-valeryl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
-
electron acceptor: electron-transferring flavoprotein
-
?
n-valeryl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
-
46% relative specific activity to isovaleryl-CoA
-
?
n-valeryl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
-
-
-
?
n-valeryl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
-
-
-
?
n-valeryl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
-
-
-
?
n-valeryl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
-
32% relative specific activity to isovaleryl-CoA
-
?
octanoyl-CoA + acceptor
oct-2-enoyl-CoA + reduced acceptor
-
7% relative activity to isovaleryl-CoA
-
?
octanoyl-CoA + acceptor
oct-2-enoyl-CoA + reduced acceptor
-
1% relative specific activity to isovaleryl-CoA
-
?
octanoyl-CoA + acceptor
oct-2-enoyl-CoA + reduced acceptor
very low activity
-
-
?
valeryl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
-
-
-
-
?
valeryl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
low activity
-
-
?
additional information
?
-
-
the presence of a putative enzyme supports functional leucine catabolism in plant mitochondria
-
-
?
additional information
?
-
activity measurement using an acyl-CoA substrate and 2,6-dichloroindophenol as an electron acceptor, with phenazinemethosulfate as an intermediate electron carrier
-
-
?
additional information
?
-
-
activity measurement using an acyl-CoA substrate and 2,6-dichloroindophenol as an electron acceptor, with phenazinemethosulfate as an intermediate electron carrier
-
-
?
additional information
?
-
activity measurement using an acyl-CoA substrate and 2,6-dichloroindophenol as an electron acceptor, with phenazinemethosulfate as an intermediate electron carrier
-
-
?
additional information
?
-
activity measurement using an acyl-CoA substrate and 2,6-dichloroindophenol as an electron acceptor, with phenazinemethosulfate as an intermediate electron carrier
-
-
?
additional information
?
-
-
substrate specificity of wild-type and mutant enzymes
-
-
?
additional information
?
-
-
deficiency of the enzyme in humans is responsible for isovaleric acidemia
-
-
?
additional information
?
-
deficiency of the enzyme in humans is responsible for isovaleric acidemia
-
-
?
additional information
?
-
-
deficiency of the enzyme in humans is responsible for isovaleric acidemia
-
-
?
additional information
?
-
-
E254 of the enzyme is in close proximity to the bound FAD, E254 is the active site catalytic residue
-
-
?
additional information
?
-
-
E254 of the enzyme is in close proximity to the bound FAD, E254 is the active site catalytic residue
-
-
?
additional information
?
-
-
the location of the catalytic residue together with a glycine at position 374 is important for conferring branched-chain substrate specificity to the enzyme
-
-
?
additional information
?
-
-
R387 has an important role in anchoring the substrate
-
-
?
additional information
?
-
-
the type III enzyme mutation responsible for isovaleric acidemia leads to a shift in reading frame and the subsequent incorporation of eight abnormally placed amino acids with premature termination of translation
-
-
?
additional information
?
-
-
a specific deficiency of enzyme activity is observed in cultured skin fibroblasts from patients with isovaleric acidemia
-
-
?
additional information
?
-
-
a specific deficiency of enzyme activity is observed in cultured skin fibroblasts from patients with isovaleric acidemia
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
-
physiological implications of enzyme mutations and deficiency
-
-
?
additional information
?
-
-
isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency
-
-
?
additional information
?
-
-
Glu-244 is the catalytic base responsible for abstracting the alpha-proton of substrate
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
no activity of LiuA with isobutyryl-CoA, 3-hydroxybutyryl-CoA, octanoyl-CoA, citronellyl-CoA or 5-methyl-hex-4-enoyl-CoA
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
the enzyme catalyzes the dehydrogenation of monomethyl branched-chain fatty acid thioester derivatives
-
-
?
additional information
?
-
broader substrate specificity, overview. The enzyme is also active with octanoyl-CoA, decanoyl-CoA, and dodecanoyl-CoA. No activity with isobutyryl-CoA and myristoyl-CoA, with DCIPIP and phenazine methosulfate as second electron acceptors
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
isovaleryl-CoA + 2,6-dichlorophenolindophenol
?
-
high substrate specificity
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
isovaleryl-CoA + electron transfer protein
3-methylcrotonoyl-CoA + reduced electron transfer protein
-
-
-
-
?
isovaleryl-CoA + electron transfer protein
3-methylcrotonyl-CoA + reduced electron transfer protein
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
isovaleryl-CoA + FAD
3-methylcrotonyl-CoA + FADH2
additional information
?
-
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
electron acceptor: electron-transfer flavoprotein serves as a natural electron acceptor for the enzyme with isovaleryl-CoA as substrate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
electron acceptor: electron-transfer flavoprotein serves as a natural electron acceptor for the enzyme with isovaleryl-CoA as substrate
-
?
isovaleryl-CoA + acceptor
3-methylcrotonyl-CoA + reduced acceptor
-
-
-
?
isovaleryl-CoA + electron transfer protein
3-methylcrotonyl-CoA + reduced electron transfer protein
-
-
-
-
?
isovaleryl-CoA + electron transfer protein
3-methylcrotonyl-CoA + reduced electron transfer protein
-
-
-
?
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
-
?
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
isovaleryl-CoA + electron-transfer flavoprotein
3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
isovaleryl-CoA + FAD
3-methylcrotonyl-CoA + FADH2
-
-
-
-
?
isovaleryl-CoA + FAD
3-methylcrotonyl-CoA + FADH2
-
-
-
?
additional information
?
-
-
the presence of a putative enzyme supports functional leucine catabolism in plant mitochondria
-
-
?
additional information
?
-
-
deficiency of the enzyme in humans is responsible for isovaleric acidemia
-
-
?
additional information
?
-
deficiency of the enzyme in humans is responsible for isovaleric acidemia
-
-
?
additional information
?
-
-
deficiency of the enzyme in humans is responsible for isovaleric acidemia
-
-
?
additional information
?
-
-
E254 of the enzyme is in close proximity to the bound FAD, E254 is the active site catalytic residue
-
-
?
additional information
?
-
-
E254 of the enzyme is in close proximity to the bound FAD, E254 is the active site catalytic residue
-
-
?
additional information
?
-
-
the location of the catalytic residue together with a glycine at position 374 is important for conferring branched-chain substrate specificity to the enzyme
-
-
?
additional information
?
-
-
R387 has an important role in anchoring the substrate
-
-
?
additional information
?
-
-
the type III enzyme mutation responsible for isovaleric acidemia leads to a shift in reading frame and the subsequent incorporation of eight abnormally placed amino acids with premature termination of translation
-
-
?
additional information
?
-
-
a specific deficiency of enzyme activity is observed in cultured skin fibroblasts from patients with isovaleric acidemia
-
-
?
additional information
?
-
-
a specific deficiency of enzyme activity is observed in cultured skin fibroblasts from patients with isovaleric acidemia
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
-
physiological implications of enzyme mutations and deficiency
-
-
?
additional information
?
-
-
isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency
-
-
?
additional information
?
-
-
Glu-244 is the catalytic base responsible for abstracting the alpha-proton of substrate
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme catalyzes the third step of the leucine oxidative metabolism
-
-
?
additional information
?
-
the enzyme catalyzes the dehydrogenation of monomethyl branched-chain fatty acid thioester derivatives
-
-
?
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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.
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
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.
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.
isovaleryl-coa dehydrogenase deficiency
Endogenous catabolism is the major source of toxic metabolites in isovaleric acidemia.
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.
isovaleryl-coa dehydrogenase deficiency
Isovaleric acidemia diagnosed promptly by tandem mass spectrometry: report of one case.
isovaleryl-coa dehydrogenase deficiency
Isovaleric acidemia with promyelocytic myeloproliferative syndrome.
isovaleryl-coa dehydrogenase deficiency
L-carnitine therapy in isovaleric acidemia.
isovaleryl-coa dehydrogenase deficiency
Long Term Follow-Up of Polish Patients with Isovaleric Aciduria. Clinical and Molecular Delineation of Isovaleric Aciduria.
isovaleryl-coa dehydrogenase deficiency
Screening for defects of branched-chain amino acid metabolism.
isovaleryl-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.
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.
Metabolic Diseases
[Pancytopenia and metabolic decompensation in a neonate].
Metabolic Syndrome
Broad connections in the Arabidopsis seed metabolic network revealed by metabolite profiling of an amino acid catabolism mutant.
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.
Neoplasms
Down-regulation of metabolic proteins in hepatocellular carcinoma with portal vein thrombosis.
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.
Seizures
Proteomic analysis of stargazer mutant mouse neuronal proteins involved in absence seizure.
Starvation
The differential impact of amino acids on OXPHOS system activity following carbohydrate starvation in Arabidopsis cell suspensions.
Thrombosis
Down-regulation of metabolic proteins in hepatocellular carcinoma with portal vein thrombosis.
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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
0.0043
-
recombinant wild-type enzyme, substrate 2-methylbutanoyl-CoA
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
0.0152
-
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
0.0472
-
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
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
2.91
-
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
0.03
-
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
-
substrate: n-butyryl-CoA
0.832
-
-
0.832
-
substrate: n-valeryl-CoA
2.68
-
-
2.68
-
substrate: isovaleryl-CoA
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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
-
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
-
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
metabolism
IVD acts in the third step of leucine degradation
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
-
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
-
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
-
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
-
IVD acts in the third step of leucine degradation
-
physiological function
involvement of ivdh in phytol degradation during dark-Induced starvation
physiological function
-
IVD catalyzes the stereospecific conversion of the diastereotopic methyl group of leucine to isoprenoidal lipids
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
-
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
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
-
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
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
-
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
residue E246 is the predicted active site catalytic residue of the enzyme
additional information
-
the enzyme reactions stereochemical course is anti-elimination
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
-
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
-
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
-
residue E246 is the predicted active site catalytic residue of the enzyme
-
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
-
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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
Y166F
mutation does not block enzyme interaction with the electron transfer protein
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
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
R363C
enzyme activity detected, 1% relative activity to wild-type
R363C
-
isovaleric acidemia is a rare recessive autosomal disorder, caused by isovaleryl-CoA dehydrogenase (IVD) deficiency. Molecular analysis of their IVD gene reveals six mutation profiles: R21H, R363C, H100R, S97F, C30Y and Y371C (common recurring missense mutation)
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
-
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
-
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
-
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
-
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
-
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
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-
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