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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

Renatured

Renatured on EC 2.3.1.12 - dihydrolipoyllysine-residue acetyltransferase

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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of E1 with E2-E3 complex with a stoichiometry of E1:E2:E3 of 2:1:1
-
reconstitution of pyruvate dehydrogenase complex
reconstitution of pyruvate dehydrogenase complex with components from Escherichia coli and Salmonella typhimurium
-
reconstitution of pyruvate dehydrogenase complex, maximum activity is produced when transacetylase accommodates 12 pyruvate dehydrogenase dimers and 6 flavoprotein dimers
-
reconstitution of pyruvate dehydrogenase complex, optimum catalytic stoichiometry of E1:E2:E3 is 5.2:11.5:2
-
reconstitution of pyruvate dehydrogenase complex, stoichiometry pyruvate dehydrogenase:transacetylase:flavoprotein is 1:0.35:0.4
-
reconstitution of the active multienzyme complex with recombinant components
-
reconstitution with components from Escherichia coli and Azotobacter vinelandii, optimum catalytic stoichiometry of E1:E2:E3 is 1:1:0.5
-
treatment with dilute acetic acid solution results in dissociation into inactive subunits with MW 70000, removal of the acid results in restoration of enzymatic activity
-
treatment with guanidine hydrochloride and its subsequent removal results in little recovery of the core, but full recovery of X
-
treatment with guanidine hydrochloride and its subsequent removal results in refolding
-
treatment with guanidine hydrochloride results in dissociation into subunits, removal of guanidine hydrochloride results in refolding of the enzyme with 95% of the original activity
-