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2.3.1.12: dihydrolipoyllysine-residue acetyltransferase

This is an abbreviated version!
For detailed information about dihydrolipoyllysine-residue acetyltransferase, go to the full flat file.

Word Map on EC 2.3.1.12

Reaction

acetyl-CoA
+
enzyme N6-(dihydrolipoyl)lysine
=
CoA
 +
enzyme N6-(S-acetyldihydrolipoyl)lysine

Synonyms

acetyltransferase, lipoate, DHLTA, dihydrolipoamide acetyltransferase, dihydrolipoate acetyltransferase, dihydrolipoic transacetylase, dihydrolipoyl acetyl transferase, dihydrolipoyl acetyltransferase, dihydrolipoyl acetyltransferase component E2, dihydrolipoyl acetyltransferase E2p, dihydrolipoyl transacetylase, dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial, DLAT, E2, E2p, hE2, Lat1, lipoate acetyltransferase, lipoate transacetylase, lipoic acetyltransferase, lipoic acid acetyltransferase, lipoic transacetylase, lipoylacetyltransferase, More, myelin-proteolipid O-palmitoyltransferase, palmitoyl-CoA:myelin-proteolipid O-palmitoyltransferase, pyruvate dehydrogenase complex component E2, pyruvate dehydrogenase complex component E2p, pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase component, thioltransacetylase A, transacetylase X

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.12 dihydrolipoyllysine-residue acetyltransferase

Purification

Purification on EC 2.3.1.12 - dihydrolipoyllysine-residue acetyltransferase

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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain mutants
-
E1-E2 complex
-
E2-E3 subcomplex of pyruvate dehydrogenase, i.e. dihydrolipoamide acetyltransferase and dehydrogenase
-
from pyruvate dehydrogenase complex
fusion protein of 6 amino acids form beta-galactosidase, the apa-4 region and the catalytic domain of E2
-
fusion protein of 6 amino acids form beta-galactosidase, the papa-4 region and the catalytic domain of E2
-
fusion protein with glutathione S-transferase
-
highly
-
isolation of lipoyl domains
-
nickel affinity column chromatography
nickel affinity resin column chromatography, Superdex G75 gel filtration, and G3000SW TSK gel filtration
peptides after limited proteolysis
-
preparation of E2-X subcomplex: E2 i.e. EC 2.3.1.12, X i.e. component X of mammalian pyruvate dehydrogenase complex
-
proteolytic fragments, isolation of lipoyl domain and catalytic domain
-
purification from pyruvate dehydrogenase complex, composed of EC 1.2.4.1, EC 1.8.1.4, EC 2.3.1.12
-
purification of pyruvate dehydrogenase complex, composed of EC 1.2.4.1, EC 1.8.1.4, EC 2.3.1.12
Hansenula miso
-
purification of the multienzyme complex
purification of tryptic fragments
-
pyruvate dehydrogenase complex and tryptic fragments of E2
-
pyruvate dehydrogenase complex, composed of EC 1.2.4.1, EC 1.8.1.4, EC 2.3.1.12
pyruvate dehydrogenase complex, composed of EC 1.2.4.1, EC 1.8.1.4. EC 2.3.1.12
-
pyruvate dehydrogenase complex, stoichiometry E1:E2:E3 is 1.56:1:0.89
-
recombinant 1-lip E2 and recombinant hybrid lipoyl domain by ammonium sulfate fractionation, ion exchange and hydrophobic interaction chromatography
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
using a sephacryl S-400 HR column
using Ni-nitrilotriacetate-agarose affinity chromatography
-
wild-type and mutants with deletions of lipolyl domains
-