Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.3.8.5 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

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

KM Value [mM]

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

Localization

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Ascaris suum O16843
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Ascaris suum

Specific Activity [micromol/min/mg]

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

Storage Stability

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

Substrates and Products (Substrate)

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

Subunits

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Ascaris suum

Cofactor

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