BRENDA - Enzyme Database show
show all sequences of 1.3.8.12

(2S)-Methylsuccinyl-CoA dehydrogenase closes the ethylmalonyl-CoA pathway for acetyl-CoA assimilation

Erb, T.J.; Fuchs, G.; Alber, B.E.; Mol. Microbiol. 73, 992-1008 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli as a N-terminal histidine-tagged fusion protein
Rhodobacter sphaeroides
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
62300
-
2 * 62300, N-terminal histidine-tagged fusion protein, SDS-PAGE
Rhodobacter sphaeroides
100000
-
gel filtration
Rhodobacter sphaeroides
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(2S)-methylsuccinyl-CoA + electron-transfer flavoprotein
Rhodobacter sphaeroides
the enzyme is involved ion the ethylmalonyl-CoA pathway for acetyl-CoA assimilation
2-methylfumaryl-CoA + reduced electron-transfer flavoprotein
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodobacter sphaeroides
D3JV03
-
-
Purification (Commentary)
Commentary
Organism
-
Rhodobacter sphaeroides
Source Tissue
Source Tissue
Commentary
Organism
Textmining
culture condition:acetate-grown cell
-
Rhodobacter sphaeroides
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2S)-methylsuccinyl-CoA + electron-transfer flavoprotein
the enzyme is involved ion the ethylmalonyl-CoA pathway for acetyl-CoA assimilation
730403
Rhodobacter sphaeroides
2-methylfumaryl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
(2S)-methylsuccinyl-CoA + electron-transfer flavoprotein
the enzyme is highly specific for (S)-methylsuccinyl-CoA. No activity with butyryl-CoA, isobutyryl-CoA or a diastereomeric mixture of (R)-methylsuccinyl-CoA
730403
Rhodobacter sphaeroides
2-methylfumaryl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
2 * 62300, N-terminal histidine-tagged fusion protein, SDS-PAGE
Rhodobacter sphaeroides
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Rhodobacter sphaeroides
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
assay at
Rhodobacter sphaeroides
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
the enzyme contains 0.7 mol of noncovalently bound FAD molecule per subunit
Rhodobacter sphaeroides
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli as a N-terminal histidine-tagged fusion protein
Rhodobacter sphaeroides
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
the enzyme contains 0.7 mol of noncovalently bound FAD molecule per subunit
Rhodobacter sphaeroides
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
62300
-
2 * 62300, N-terminal histidine-tagged fusion protein, SDS-PAGE
Rhodobacter sphaeroides
100000
-
gel filtration
Rhodobacter sphaeroides
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(2S)-methylsuccinyl-CoA + electron-transfer flavoprotein
Rhodobacter sphaeroides
the enzyme is involved ion the ethylmalonyl-CoA pathway for acetyl-CoA assimilation
2-methylfumaryl-CoA + reduced electron-transfer flavoprotein
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Rhodobacter sphaeroides
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
culture condition:acetate-grown cell
-
Rhodobacter sphaeroides
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2S)-methylsuccinyl-CoA + electron-transfer flavoprotein
the enzyme is involved ion the ethylmalonyl-CoA pathway for acetyl-CoA assimilation
730403
Rhodobacter sphaeroides
2-methylfumaryl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
(2S)-methylsuccinyl-CoA + electron-transfer flavoprotein
the enzyme is highly specific for (S)-methylsuccinyl-CoA. No activity with butyryl-CoA, isobutyryl-CoA or a diastereomeric mixture of (R)-methylsuccinyl-CoA
730403
Rhodobacter sphaeroides
2-methylfumaryl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 62300, N-terminal histidine-tagged fusion protein, SDS-PAGE
Rhodobacter sphaeroides
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Rhodobacter sphaeroides
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
assay at
Rhodobacter sphaeroides
General Information
General Information
Commentary
Organism
metabolism
the enzyme is involved in the ethylmalonyl-CoA pathway, an acetyl-CoA assimilation strategy
Rhodobacter sphaeroides
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme is involved in the ethylmalonyl-CoA pathway, an acetyl-CoA assimilation strategy
Rhodobacter sphaeroides
Other publictions for EC 1.3.8.12
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
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)
730403
Erb
(2S)-Methylsuccinyl-CoA dehydr ...
Rhodobacter sphaeroides
Mol. Microbiol.
73
992-1008
2009
-
-
1
-
-
-
-
-
-
-
2
1
-
5
-
-
1
-
-
1
-
-
2
1
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
2
1
-
-
-
1
-
1
-
-
2
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-