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Literature summary for 2.3.1.61 extracted from

  • Andi, B.; Soares, A.S.; Shi, W.; Fuchs, M.R.; McSweeney, S.; Liu, Q.
    Structure of the dihydrolipoamide succinyltransferase catalytic domain from Escherichia coli in a novel crystal form a tale of a common protein crystallization contaminant (2019), Acta Crystallogr. Sect. F, 75, 616-624 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
catalytic domain, hanging drop vapor diffusion method, using 1 M sodium acetate, 50 mM cadmium sulfate, 50 mM HEPES pH 7.5 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
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AFG6
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA resin column chromatography 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
-
?

Subunits

Subunits Comment Organism
? x * 44000, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
dihydrolipoamide succinyltransferase
-
Escherichia coli
DSCD catalytic enzyme domain Escherichia coli