Literature summary extracted from
Chakraborty, J.; Nemeria, N.S.; Farinas, E.; Jordan, F.
Catalysis of transthiolacylation in the active centers of dihydrolipoamide acyltransacetylase components of 2-oxo acid dehydrogenase complexes (2018), FEBS Open Bio, 8, 880-896 .
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.3.1.61 |
expressed in Escherichia coli BL21(DE3) cells |
Escherichia coli |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.3.1.61 |
D374A |
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 2.1% compared to the wild type enzyme |
Escherichia coli |
2.3.1.61 |
D374N |
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 9.7% compared to the wild type enzyme |
Escherichia coli |
2.3.1.61 |
D379A |
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 9.5% compared to the wild type enzyme |
Escherichia coli |
2.3.1.61 |
H375A |
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by 2fold compared to the wild type enzyme |
Escherichia coli |
2.3.1.61 |
H375C |
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 1% compared to the wild type enzyme |
Escherichia coli |
2.3.1.61 |
H375G |
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by 5fold compared to the wild type enzyme |
Escherichia coli |
2.3.1.61 |
H375N |
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 0.5% compared to the wild type enzyme |
Escherichia coli |
2.3.1.61 |
H375W |
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by 54fold compared to the wild type enzyme |
Escherichia coli |
2.3.1.61 |
R376A |
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 56% compared to the wild type enzyme |
Escherichia coli |
2.3.1.61 |
T323A |
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 45% compared to the wild type enzyme |
Escherichia coli |
2.3.1.61 |
T323S |
the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 43% compared to the wild type enzyme |
Escherichia coli |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.3.1.61 |
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine |
Escherichia coli |
- |
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine |
- |
r |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.3.1.61 |
Escherichia coli |
P0AFG6 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.3.1.61 |
Ni-Sepharose 6 column chromatography and Sephacryl S-300 gel filtration |
Escherichia coli |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.3.1.61 |
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine |
- |
Escherichia coli |
CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine |
- |
r |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.3.1.61 |
? |
x * 11420, lipoyl domain, calculated from amino acid sequence |
Escherichia coli |
2.3.1.61 |
? |
x * 11421, lipoyl domain, mass spectrometry |
Escherichia coli |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.3.1.61 |
dihydrolipoamide acyltransacetylase |
- |
Escherichia coli |
2.3.1.61 |
E2o |
component of the 2-oxoglutarate dehydrogenase complex |
Escherichia coli |