Literature summary for 2.3.1.61 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 .

Search for more literature for 2.3.1.61

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21(DE3) cells	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
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
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
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
H375A	the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by 2fold compared to the wild type enzyme	Escherichia coli
H375C	the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 1% compared to the wild type enzyme	Escherichia coli
H375G	the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by 5fold compared to the wild type enzyme	Escherichia coli
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
H375W	the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by 54fold compared to the wild type enzyme	Escherichia coli
R376A	the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 56% compared to the wild type enzyme	Escherichia coli
T323A	the substitution decreases the catalytic efficiency of the 2-oxoglutarate dehydrogenase complex by to 45% compared to the wild type enzyme	Escherichia coli
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)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine	Escherichia coli	-	CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine	-	r

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AFG6	-	-

Purification (Commentary)

Purification (Comment)	Organism
Ni-Sepharose 6 column chromatography and Sephacryl S-300 gel filtration	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine	-	Escherichia coli	CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine	-	r

Subunits

Subunits	Comment	Organism
?	x * 11420, lipoyl domain, calculated from amino acid sequence	Escherichia coli
?	x * 11421, lipoyl domain, mass spectrometry	Escherichia coli

Synonyms

Synonyms	Comment	Organism
dihydrolipoamide acyltransacetylase	-	Escherichia coli
E2o	component of the 2-oxoglutarate dehydrogenase complex	Escherichia coli

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Release 2023.1 (January 2023)