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Literature summary for 2.3.1.168 extracted from

  • Chuang, J.L.; Davie, J.R.; Wynn, R.M.; Chuang, D.T.
    Production of recombinant mammalian holo-E2 and E3 and reconstitution of functional branched-chain alpha-keto acid dehydrogenase complex with recombinant E1 (2000), Methods Enzymol., 324, 192-200.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of apo-enzyme in Escherichia coli strain XL1-Blue, can be lipoylated in vitro Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant apo-enzyme E2 from Escherichia coli strain XL1-Blue Bos taurus

Reaction

Reaction Comment Organism Reaction ID
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine the active site is located in the inner core domain Bos taurus

Renatured (Commentary)

Renatured (Comment) Organism
recombinant apo-E2 is unable to reconstitute with recombinant E1 and E3 to an active branched-chain alpha-keto dehydrogenase, but recombinant holo-E2 is able to Bos taurus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.173
-
purified recombinant apo-enzyme Bos taurus
0.185
-
purified native enzyme Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine recombinant apo-E2 devoid of lipoic acid is fully active Bos taurus CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
?

Subunits

Subunits Comment Organism
More recombinant apo-E2 is unable to reconstitute with recombinant E1 and E3 to an active branched-chain alpha-keto dehydrogenase, but recombinant holo-E2 is able to Bos taurus

Synonyms

Synonyms Comment Organism
More enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase Bos taurus