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Literature summary extracted from

  • Komuniecki, R.; Fekete, S.; Thissen-Parra, J.
    Purification and characterization of the 2-methyl branched-chain acyl-CoA dehydrogenase, an enzyme involved in NADH-dependent enoyl-CoA reduction in anaerobic mitochondria of the nematode, Ascaris suum (1985), J. Biol. Chem., 260, 4770-4777.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.8.5 (E)-2-methyl-2-butenoyl-CoA
-
 Ascaris suum
1.3.8.5 acetoacetyl-CoA
-
 Ascaris suum
1.3.8.5 Ag2+
-
 Ascaris suum
1.3.8.5 crotonyl-CoA
-
 Ascaris suum
1.3.8.5 decanoyl-CoA
-
 Ascaris suum
1.3.8.5 hexanoyl-CoA
-
 Ascaris suum
1.3.8.5 Hg2+
-
 Ascaris suum
1.3.8.5 NEM little effect Ascaris suum
1.3.8.5 p-hydroxymercuribenzoate little effect Ascaris suum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.8.5 0.018
-
 2-methylbutanoyl-CoA
-
 Ascaris suum
1.3.8.5 0.021
-
 2-methylpentanoyl-CoA
-
 Ascaris suum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.8.5 mitochondrion
-
 Ascaris suum 5739
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.8.5 42500
-
 4 * 42500, SDS-PAGE Ascaris suum
1.3.8.5 170000
-
 gel filtration Ascaris suum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.8.5 additional information Ascaris suum 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 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.8.5 Ascaris suum O16843
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.8.5
-
 Ascaris suum

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.8.5 1.58
-
 2-methylpentanoyl-CoA Ascaris suum
1.3.8.5 1.62
-
 2-methylbutanoyl-CoA Ascaris suum

Storage Stability

EC Number Storage Stability Organism
1.3.8.5 -20°C, 50 mM potassium phosphate buffer, pH 7.4, 10% glycerol, stable for at least 30 days Ascaris suum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.8.5 2-methylbutanoyl-CoA + electron-transfer flavoprotein
-
 Ascaris suum (E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
-
 ?
1.3.8.5 2-methylpentanoyl-CoA + electron-transfer flavoprotein 98% of the activity with 2-methylbutanoyl-CoA Ascaris suum 2-methyl-2-pentenoyl-CoA + reduced electron-transfer flavoprotein + H+
-
 ?
1.3.8.5 butyryl-CoA + electron-transfer flavoprotein 13.6% of the activity with 2-methylbutanoyl-CoA Ascaris suum ? + reduced electron-transfer flavoprotein + H+
-
 ?
1.3.8.5 additional information no reaction with: propionyl-CoA, isobutanoyl-CoA, isopentanoyl-CoA, palmitoyl-CoA Ascaris suum ?
-
 ?
1.3.8.5 additional information 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 Ascaris suum ?
-
 ?
1.3.8.5 octanoyl-CoA + electron-transfer flavoprotein 12.8% of the activity with 2-methylbutanoyl-CoA Ascaris suum ? + reduced electron-transfer flavoprotein + H+
-
 ?
1.3.8.5 pentanoyl-CoA + electron-transfer flavoprotein 14.4% of the activity with 2-methylbutanoyl-CoA Ascaris suum ? + reduced electron-transfer flavoprotein + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.8.5 tetramer 4 * 42500, SDS-PAGE Ascaris suum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.8.5 7.5
-
-
 Ascaris suum

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.8.5 FAD contains 0.9 mol of FAD per mol of subunit Ascaris suum