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Information on EC 1.3.8.5 - short-chain 2-methylacyl-CoA dehydrogenase
for references in articles please use BRENDA:EC1.3.8.5
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EC Tree 1 Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.8 With a flavin as acceptor
1.3.8.5 short-chain 2-methylacyl-CoA dehydrogenase
IUBMB Comments
A flavoprotein (FAD). The mammalian enzyme catalyses an oxidative reaction as a step in the mitochondrial β-oxidation of short-chain 2-methyl fatty acids and participates in isoleucine degradation. The enzyme from the parasitic helminth Ascaris suum catalyses a reductive reaction as part of a fermentation pathway, shuttling reducing power from the electron-transport chain to 2-methyl branched-chain enoyl CoA.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.3.8.5
- acylcarnitine
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acadsb
- isobutyryl-coa
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dehydrogenation
- isovaleryl-coa
- acidemia
-
isovaleric
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inborn
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hmong
- l-isoleucine
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ascarid
- isovalerylcarnitine
- acylglycine
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wisconsin
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submitochondrial
Reaction Schemes
showSynonyms
sbcad, sbcadd, short/branched chain acyl-coa dehydrogenase, 2-methylbutyryl-coa dehydrogenase, 2mbcd, 2-methyl branched-chain acyl-coa dehydrogenase, 2-methyl branched-chain enoyl-coa reductase, 2-methyl branched-chain enoyl coa reductase, 2-methyl branched chain acyl-coa dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-methyl branched chain acyl-CoA dehydrogenase
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2-Methyl branched-chain acyl-CoA dehydrogenase
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2-Methyl branched-chain enoyl CoA reductase
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2-Methyl branched-chain enoyl-CoA reductase
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branched chain acyl-CoA dehydrogenase
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EC 1.3.99.12
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-
formerly
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ECR
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-
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Methyl branched-chain enoyl-CoA reductase
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Reductase, methyl branched-chain enoyl coenzyme A
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SBCAD
short/branched chain acyl-CoA dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-methylbutanoyl-CoA + electron-transfer flavoprotein = (E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
2-methylbutanoyl-CoA + electron-transfer flavoprotein = (E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
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2-methylbutanoyl-CoA + electron-transfer flavoprotein = (E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
reaction mechanism determining substrate specificity
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2-methylbutanoyl-CoA + electron-transfer flavoprotein = (E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
reaction mechanism determining substrate specificity
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2-methylbutanoyl-CoA + electron-transfer flavoprotein = (E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
the isovaleryl-CoA dehydrogenase 1, i.e. IVD1, EC 1.3.99.10, from Solanum tuberosum shows maximal activity with 2-methylbutyryl-CoA, the binding pockets of 2-methylbutyryl-CoA and isovaleryl-CoA dehydrogenase are nearly identical, the enzyme therefore shall also be classified to EC 1.3.99.12, active site structure, residues Met361, Ala365, Val88, Val92, and Val96 are involved in catalysis
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
2-methyl-branched fatty acid beta-oxidation, L-isoleucine degradation I, L-valine degradation I, propanoate fermentation to 2-methylbutanoate, valproate beta-oxidation
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SYSTEMATIC NAME
IUBMB Comments
short-chain 2-methylacyl-CoA:electron-transfer flavoprotein 2-oxidoreductase
A flavoprotein (FAD). The mammalian enzyme catalyses an oxidative reaction as a step in the mitochondrial beta-oxidation of short-chain 2-methyl fatty acids and participates in isoleucine degradation. The enzyme from the parasitic helminth Ascaris suum catalyses a reductive reaction as part of a fermentation pathway, shuttling reducing power from the electron-transport chain to 2-methyl branched-chain enoyl CoA.
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CAS REGISTRY NUMBER
COMMENTARY
122320-06-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-2-methylbutanoyl-CoA + electron-transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
(S)-2-methylbutanoyl-CoA + acceptor
2-methylbut-2-enoyl-CoA + reduced acceptor
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Substrates: acceptors: electron transfer flavoprotein, phenazine methosulfate, meldola's blue
Products: -
Products: -
r
(S)-2-methylbutanoyl-CoA + electron-transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
2-methylbutanoyl-CoA + electron transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron transfer flavoprotein
2-methylbutanoyl-CoA + electron-transfer flavoprotein
(E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
Substrates: -
Products: -
Products: -
?
2-methylpentanoyl-CoA + electron-transfer flavoprotein
2-methyl-2-pentenoyl-CoA + reduced electron-transfer flavoprotein + H+
Substrates: 98% of the activity with 2-methylbutanoyl-CoA
Products: -
Products: -
?
butyryl-CoA + acceptor
2-butenoyl-CoA + reduced acceptor
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Substrates: 5% of activity with 2-methylbutyryl-CoA
Products: -
Products: -
?
butyryl-CoA + electron-transfer flavoprotein
? + reduced electron-transfer flavoprotein + H+
Substrates: 13.6% of the activity with 2-methylbutanoyl-CoA
Products: -
Products: -
?
butyryl-CoA + electron-transfer flavoprotein
but-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
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Substrates: -
Products: -
Products: -
?
hexanoyl-CoA + electron-transfer flavoprotein
hex-2-enoyl-CoA + reduced electron-transfer flavoprotein
isobutyryl-CoA + acceptor
methacrylyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
isobutyryl-CoA + electron-transfer flavoprotein
2-methylacryloyl-CoA + reduced electron-transfer flavoprotein + H+
octanoyl-CoA + electron-transfer flavoprotein
? + reduced electron-transfer flavoprotein + H+
Substrates: 12.8% of the activity with 2-methylbutanoyl-CoA
Products: -
Products: -
?
octanoyl-CoA + electron-transfer flavoprotein
oct-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
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Substrates: -
Products: -
Products: -
?
pentanoyl-CoA + electron-transfer flavoprotein
? + reduced electron-transfer flavoprotein + H+
Substrates: 14.4% of the activity with 2-methylbutanoyl-CoA
Products: -
Products: -
?
valeryl-CoA + electron-transfer flavoprotein
pent-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
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Substrates: -
Products: -
Products: -
?
(R)-2-methylbutanoyl-CoA + electron-transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
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Substrates: -
Products: i.e. ethylacrylyl-CoA
Products: i.e. ethylacrylyl-CoA
?
(R)-2-methylbutanoyl-CoA + electron-transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
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Substrates: involved in the (S)-pathway of L-isoleucine oxidation, and also in the (R)-pathway of L-alloisoleucine oxidation due to interconvertion of the 3 isomers
Products: -
Products: -
?
(R)-2-methylbutyryl-CoA + acceptor
2-ethylprop-2-enoyl-CoA + reduced acceptor
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Substrates: -
Products: -
Products: -
?
(R)-2-methylbutyryl-CoA + acceptor
2-ethylprop-2-enoyl-CoA + reduced acceptor
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Substrates: 22% of activity with (S)-2-methylbutyryl-CoA
Products: -
Products: -
?
(S)-2-methylbutanoyl-CoA + electron-transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
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Substrates: -
Products: -
Products: -
?
(S)-2-methylbutanoyl-CoA + electron-transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
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Substrates: -
Products: i.e. tiglyl-CoA
Products: i.e. tiglyl-CoA
?
(S)-2-methylbutanoyl-CoA + electron-transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
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Substrates: involved in the (S)-pathway of L-isoleucine oxidation, and also in the (R)-pathway of L-alloisoleucine oxidation due to interconvertion of the 3 isomers
Products: -
Products: -
?
(S)-2-methylbutanoyl-CoA + electron-transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
-
Substrates: -
Products: -
Products: -
?
2-methylbutanoyl-CoA + electron transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron transfer flavoprotein
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Substrates: -
Products: -
Products: -
r
2-methylbutanoyl-CoA + electron transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron transfer flavoprotein
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Substrates: enzyme catalyzes the third step in the oxidative metabolism of isoleucin and valine
Products: -
Products: -
r
2-methylbutanoyl-CoA + electron transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
hexanoyl-CoA + electron-transfer flavoprotein
hex-2-enoyl-CoA + reduced electron-transfer flavoprotein
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Substrates: 41% of activity with (S)-2-methylbutanoyl-CoA
Products: -
Products: -
?
hexanoyl-CoA + electron-transfer flavoprotein
hex-2-enoyl-CoA + reduced electron-transfer flavoprotein
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Substrates: 8% of activity with (S)-2-methylbutanoyl-CoA, wild-type enzyme
Products: -
Products: -
?
hexanoyl-CoA + electron-transfer flavoprotein
hex-2-enoyl-CoA + reduced electron-transfer flavoprotein
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Substrates: -
Products: -
Products: -
?
isobutyryl-CoA + electron-transfer flavoprotein
2-methylacryloyl-CoA + reduced electron-transfer flavoprotein + H+
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Substrates: 6% of activity with (S)-2-methylbutanoyl-CoA
Products: -
Products: -
?
isobutyryl-CoA + electron-transfer flavoprotein
2-methylacryloyl-CoA + reduced electron-transfer flavoprotein + H+
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Substrates: 37% of activity with (S)-2-methylbutanoyl-CoA, wild-type enzyme
Products: -
Products: -
?
additional information
?
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Substrates: no reaction with: propionyl-CoA, isobutanoyl-CoA, isopentanoyl-CoA, palmitoyl-CoA
Products: -
Products: -
?
additional information
?
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Substrates: no reaction with: propionyl-CoA, isobutanoyl-CoA, isopentanoyl-CoA, palmitoyl-CoA
Products: -
Products: -
?
additional information
?
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Substrates: the enzyme plays a pivotal role in the reversal of beta-oxidation operating in anaerobic mitochondria of the parasitic nematode Ascaris suum
Products: -
Products: -
?
additional information
?
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Substrates: the enzyme plays a pivotal role in the reversal of beta-oxidation operating in anaerobic mitochondria of the parasitic nematode Ascaris suum
Products: -
Products: -
?
additional information
?
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Substrates: the enzyme plays a pivotal role in the reversal of beta-oxidation operating in anaerobic mitochondria of the parasitic nematode Ascaris suum
Products: -
Products: -
?
additional information
?
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Substrates: the electron-transport chain of the organism and the enzyme 2-methyl-branched-chain-enoyl-CoA reductase are responsible for the NADH-dependent reduction of the branched-chain enoyl-CoAs observed in mitochondria
Products: -
Products: -
?
additional information
?
-
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Substrates: the electron-transport chain of the organism and the enzyme 2-methyl-branched-chain-enoyl-CoA reductase are responsible for the NADH-dependent reduction of the branched-chain enoyl-CoAs observed in mitochondria
Products: -
Products: -
?
additional information
?
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Substrates: expression of the enzyme is tissue-specific and developmentally regulated
Products: -
Products: -
?
additional information
?
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Substrates: enzyme deficiency causes 2-ethylhydracrylic aciduria with excretion f 2-methylbutyrylglycine
Products: -
Products: -
?
additional information
?
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Substrates: substrate specificity of wild-type and mutants, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with isovaleryl-CoA
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-2-methylbutanoyl-CoA + electron-transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
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Substrates: involved in the (S)-pathway of L-isoleucine oxidation, and also in the (R)-pathway of L-alloisoleucine oxidation due to interconvertion of the 3 isomers
Products: -
Products: -
?
(S)-2-methylbutanoyl-CoA + electron-transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
-
Substrates: involved in the (S)-pathway of L-isoleucine oxidation, and also in the (R)-pathway of L-alloisoleucine oxidation due to interconvertion of the 3 isomers
Products: -
Products: -
?
2-methylbutanoyl-CoA + electron transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron transfer flavoprotein
2-methylbutanoyl-CoA + electron transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
r
2-methylbutanoyl-CoA + electron transfer flavoprotein
2-methylbut-2-enoyl-CoA + reduced electron transfer flavoprotein
-
Substrates: enzyme catalyzes the third step in the oxidative metabolism of isoleucin and valine
Products: -
Products: -
r
additional information
?
-
-
Substrates: the enzyme plays a pivotal role in the reversal of beta-oxidation operating in anaerobic mitochondria of the parasitic nematode Ascaris suum
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays a pivotal role in the reversal of beta-oxidation operating in anaerobic mitochondria of the parasitic nematode Ascaris suum
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays a pivotal role in the reversal of beta-oxidation operating in anaerobic mitochondria of the parasitic nematode Ascaris suum
Products: -
Products: -
?
additional information
?
-
Substrates: the electron-transport chain of the organism and the enzyme 2-methyl-branched-chain-enoyl-CoA reductase are responsible for the NADH-dependent reduction of the branched-chain enoyl-CoAs observed in mitochondria
Products: -
Products: -
?
additional information
?
-
-
Substrates: the electron-transport chain of the organism and the enzyme 2-methyl-branched-chain-enoyl-CoA reductase are responsible for the NADH-dependent reduction of the branched-chain enoyl-CoAs observed in mitochondria
Products: -
Products: -
?
additional information
?
-
-
Substrates: expression of the enzyme is tissue-specific and developmentally regulated
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme deficiency causes 2-ethylhydracrylic aciduria with excretion f 2-methylbutyrylglycine
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(methylenecyclopropyl)acetyl-CoA
-
0.0025 mM, slow inhibition, half-time approx. 30 min
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
acyl-coa dehydrogenase deficiency
2-methylbutyryl-CoA dehydrogenase deficiency associated with autism and mental retardation: a case report.
acyl-coa dehydrogenase deficiency
Acylglycine Analysis by Ultra-Performance Liquid Chromatography-Tandem Mass Spectrometry (UPLC-MS/MS).
acyl-coa dehydrogenase deficiency
Biochemical, Clinical, and Genetic Characteristics of Short/Branched Chain Acyl-CoA Dehydrogenase Deficiency in Chinese Patients by Newborn Screening.
acyl-coa dehydrogenase deficiency
Prevalence and mutation analysis of short/branched chain acyl-CoA dehydrogenase deficiency (SBCADD) detected on newborn screening in Wisconsin.
Intellectual Disability
2-methylbutyryl-CoA dehydrogenase deficiency associated with autism and mental retardation: a case report.
Maple Syrup Urine Disease
Advances and challenges in the treatment of branched-chain amino/keto acid metabolic defects.
medium-chain acyl-coa dehydrogenase deficiency
Acylglycine Analysis by Ultra-Performance Liquid Chromatography-Tandem Mass Spectrometry (UPLC-MS/MS).
methylcrotonoyl-coa carboxylase deficiency
Acylglycine Analysis by Ultra-Performance Liquid Chromatography-Tandem Mass Spectrometry (UPLC-MS/MS).
Multiple Acyl Coenzyme A Dehydrogenase Deficiency
Acylglycine Analysis by Ultra-Performance Liquid Chromatography-Tandem Mass Spectrometry (UPLC-MS/MS).
Propionic Acidemia
Acylglycine Analysis by Ultra-Performance Liquid Chromatography-Tandem Mass Spectrometry (UPLC-MS/MS).
Propionic Acidemia
Advances and challenges in the treatment of branched-chain amino/keto acid metabolic defects.
Seizures
Short/branched-chain acyl-CoA dehydrogenase deficiency due to an IVS3+3A>G mutation that causes exon skipping.
short-chain 2-methylacyl-coa dehydrogenase deficiency
2-methylbutyryl-CoA dehydrogenase deficiency associated with autism and mental retardation: a case report.
short-chain 2-methylacyl-coa dehydrogenase deficiency
2-methylbutyryl-CoA dehydrogenase deficiency in Hmong infants identified by expanded newborn screen.
short-chain 2-methylacyl-coa dehydrogenase deficiency
2-Methylbutyrylglycine induces lipid oxidative damage and decreases the antioxidant defenses in rat brain.
short-chain 2-methylacyl-coa dehydrogenase deficiency
Acylglycine Analysis by Ultra-Performance Liquid Chromatography-Tandem Mass Spectrometry (UPLC-MS/MS).
short-chain 2-methylacyl-coa dehydrogenase deficiency
Advances and challenges in the treatment of branched-chain amino/keto acid metabolic defects.
short-chain 2-methylacyl-coa dehydrogenase deficiency
Biochemical, Clinical, and Genetic Characteristics of Short/Branched Chain Acyl-CoA Dehydrogenase Deficiency in Chinese Patients by Newborn Screening.
short-chain 2-methylacyl-coa dehydrogenase deficiency
Characterization of new ACADSB gene sequence mutations and clinical implications in patients with 2-methylbutyrylglycinuria identified by newborn screening.
short-chain 2-methylacyl-coa dehydrogenase deficiency
Clinical, biochemical, and molecular spectrum of short/branched-chain acyl-CoA dehydrogenase deficiency: two new cases and review of literature.
short-chain 2-methylacyl-coa dehydrogenase deficiency
Inborn errors of isoleucine degradation: a review.
short-chain 2-methylacyl-coa dehydrogenase deficiency
Prevalence and mutation analysis of short/branched chain acyl-CoA dehydrogenase deficiency (SBCADD) detected on newborn screening in Wisconsin.
short-chain 2-methylacyl-coa dehydrogenase deficiency
Prospective diagnosis of 2-methylbutyryl-CoA dehydrogenase deficiency in the Hmong population by newborn screening using tandem mass spectrometry.
short-chain 2-methylacyl-coa dehydrogenase deficiency
UPLC-MS/MS analysis of C5-acylcarnitines in dried blood spots.
short-chain acyl-coa dehydrogenase deficiency
Acylglycine Analysis by Ultra-Performance Liquid Chromatography-Tandem Mass Spectrometry (UPLC-MS/MS).
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.345
2.476
additional information
additional information
-
activity of wild-type and mutant enzymes with different substrates, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
not detected in: early, aerobic larval stages or adult testis, ovary, or intstine
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (132 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
170000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
additional information
-
structure-function relationship, molecular modeling