BRENDA - Enzyme Database
show all sequences of 1.3.8.5

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

Komuniecki, R.; Fekete, S.; Thissen-Parra, J.; J. Biol. Chem. 260, 4770-4777 (1985)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
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
Commentary
Organism
Structure
0.018
-
2-methylbutanoyl-CoA
-
Ascaris suum
0.021
-
2-methylpentanoyl-CoA
-
Ascaris suum
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Ascaris suum
5739
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42500
-
4 * 42500, SDS-PAGE
Ascaris suum
170000
-
gel filtration
Ascaris suum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
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
Commentary
Textmining
Ascaris suum
O16843
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Ascaris suum
Specific Activity [micromol/min/mg]
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
2-methylbutanoyl-CoA + electron-transfer flavoprotein
-
12302
Ascaris suum
(E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
-
12302
Ascaris suum
-
2-methylpentanoyl-CoA + electron-transfer flavoprotein
98% of the activity with 2-methylbutanoyl-CoA
12302
Ascaris suum
2-methyl-2-pentenoyl-CoA + reduced electron-transfer flavoprotein + H+
-
12302
Ascaris suum
-
butyryl-CoA + electron-transfer flavoprotein
13.6% of the activity with 2-methylbutanoyl-CoA
12302
Ascaris suum
? + reduced electron-transfer flavoprotein + H+
-
-
-
-
additional information
no reaction with: propionyl-CoA, isobutanoyl-CoA, isopentanoyl-CoA, palmitoyl-CoA
12302
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
12302
Ascaris suum
?
-
-
-
-
octanoyl-CoA + electron-transfer flavoprotein
12.8% of the activity with 2-methylbutanoyl-CoA
12302
Ascaris suum
? + reduced electron-transfer flavoprotein + H+
-
-
-
-
pentanoyl-CoA + electron-transfer flavoprotein
14.4% of the activity with 2-methylbutanoyl-CoA
12302
Ascaris suum
? + reduced electron-transfer flavoprotein + H+
-
-
-
-
Subunits
Subunits
Commentary
Organism
tetramer
4 * 42500, SDS-PAGE
Ascaris suum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Ascaris suum
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
contains 0.9 mol of FAD per mol of subunit
Ascaris suum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
contains 0.9 mol of FAD per mol of subunit
Ascaris suum
Inhibitors (protein specific)
Inhibitors
Commentary
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] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.018
-
2-methylbutanoyl-CoA
-
Ascaris suum
0.021
-
2-methylpentanoyl-CoA
-
Ascaris suum
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Ascaris suum
5739
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42500
-
4 * 42500, SDS-PAGE
Ascaris suum
170000
-
gel filtration
Ascaris suum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
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
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
-
Ascaris suum
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
1.58
-
2-methylpentanoyl-CoA
Ascaris suum
1.62
-
2-methylbutanoyl-CoA
Ascaris suum
Storage Stability (protein specific)
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) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
2-methylbutanoyl-CoA + electron-transfer flavoprotein
-
12302
Ascaris suum
(E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
-
12302
Ascaris suum
-
2-methylpentanoyl-CoA + electron-transfer flavoprotein
98% of the activity with 2-methylbutanoyl-CoA
12302
Ascaris suum
2-methyl-2-pentenoyl-CoA + reduced electron-transfer flavoprotein + H+
-
12302
Ascaris suum
-
butyryl-CoA + electron-transfer flavoprotein
13.6% of the activity with 2-methylbutanoyl-CoA
12302
Ascaris suum
? + reduced electron-transfer flavoprotein + H+
-
-
-
-
additional information
no reaction with: propionyl-CoA, isobutanoyl-CoA, isopentanoyl-CoA, palmitoyl-CoA
12302
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
12302
Ascaris suum
?
-
-
-
-
octanoyl-CoA + electron-transfer flavoprotein
12.8% of the activity with 2-methylbutanoyl-CoA
12302
Ascaris suum
? + reduced electron-transfer flavoprotein + H+
-
-
-
-
pentanoyl-CoA + electron-transfer flavoprotein
14.4% of the activity with 2-methylbutanoyl-CoA
12302
Ascaris suum
? + reduced electron-transfer flavoprotein + H+
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 42500, SDS-PAGE
Ascaris suum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
-
Ascaris suum
Other publictions for EC 1.3.8.5
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [░C]
Temperature Range [░C]
Temperature Stability [░C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [░C] (protein specific)
Temperature Range [░C] (protein specific)
Temperature Stability [░C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
12305
Duran
Developmental and tissue-speci ...
Ascaris suum
Mol. Biochem. Parasitol.
91
307-318
1998
-
-
1
-
-
-
-
-
2
-
1
2
-
3
-
-
-
-
-
4
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
1
2
-
-
-
-
-
4
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
12303
Mei
Localization of cytochrome oxi ...
Ascaris suum
J. Parasitol.
83
760-763
1997
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
12306
Duran
-
Characterization of enoly CoA ...
Ascaris suum
Diss. Abstr. Int.
57
670
1997
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
12304
Duran
Characterization of cDNA clone ...
Ascaris suum
J. Biol. Chem.
268
22391-22396
1993
-
-
1
-
-
-
-
-
4
-
1
1
-
4
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
4
-
1
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
12302
Komuniecki
Purification and characterizat ...
Ascaris suum
J. Biol. Chem.
260
4770-4777
1985
-
-
-
-
-
-
9
2
3
-
2
1
-
3
-
-
1
-
-
-
2
1
7
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
9
-
2
3
-
2
1
-
-
-
1
-
-
2
1
7
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-