2.3.1.12	acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine	-	Homo sapiens	CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine	-	?	379119	
2.3.1.12	acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine	-	Escherichia coli	CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine	-	?	379119	
2.3.1.12	acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine	-	Escherichia coli	CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine	-	r	379119	
2.3.1.12	acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine	reductive acetylation of the enzyme	Escherichia coli	CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine	-	?	379119	
2.3.1.12	CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine	-	Escherichia coli	acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine	-	r	435412	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Salmonella enterica subsp. enterica serovar Typhimurium	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Mammalia	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Bacillus subtilis	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Mus musculus	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Escherichia coli	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Homo sapiens	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Rattus norvegicus	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Sus scrofa	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Saccharomyces cerevisiae	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Bos taurus	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Bos taurus	S-acetyldihydrolipoamide + CoA	-	r	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Geobacillus stearothermophilus	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Neurospora crassa	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Solanum tuberosum	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Arabidopsis thaliana	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Neisseria meningitidis	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Azotobacter vinelandii	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Rhodospirillum rubrum	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Brassica oleracea	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Columba sp.	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Hansenula miso	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Brassica oleracea var. botrytis	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Syntrophotalea carbinolica	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	-	Zea mays	S-acetyldihydrolipoamide + CoA	-	?	320377	
2.3.1.12	dihydrolipoamide + acetyl-CoA	acetyl group is transferred from the S-acetyldihydrolipoyl moiety bound covalently to the transacetylase to CoA	Bos taurus	S-acetyldihydrolipoamide + CoA	-	r	320377	
2.3.1.12	additional information	protein bound acetyldihydrolipoyl moiety + CoA	Syntrophotalea carbinolica	?	-	?	89	
2.3.1.12	additional information	E2 plays a central role in organization, integrated chemical reactions, and regulation of the multienzyme complex, overview, binding and activation of regulatory enzyme pyruvate dehydrogenase kinase isozymes PDK1-4, the enzyme mediates Ca2+-activation of isozymes of pyruvate dehydrogenase phosphatase severalfold, and enhances the accessibility of the E1 substrate for the regulatory enzymes, and mediate feedback effector control by NADH and acetyl-CoA, and modifies the allosteric control, mechanism, overview	Homo sapiens	?	-	?	89	
2.3.1.12	additional information	E2 plays a central role in organization, integrated chemical reactions, and regulation of the multienzyme complex, overview, binding and activation of regulatory enzyme pyruvate dehydrogenase kinase isozymes PDK1-4, the enzyme mediates Ca2+-activation of isozymes of pyruvate dehydrogenase phosphatase severalfold, and enhances the accessibility of the E1 substrate for the regulatory enzymes, and mediate feedback effector control by NADH and acetyl-CoA, and modifies the allosteric control, mechanism, overview	Rattus norvegicus	?	-	?	89	
2.3.1.12	additional information	the enzyme E2 has an enormous impact on pyruvate dehydrogenase kinase PDK phosphorylation of the pyruvate dehydrogenase E1 component by acting as a mobile binding framework and in facilitating and mediating regulation of PDK activity, isozyme PDK2 interacts very weakly with L2 domain of E2, but much tighter with the recombinant dimeric glutathione S-transferase-L2 domain fusion protein, importance of bifunctional binding, interaction of PDK2 with the lipoyl domains L1 and L2 of E2, and the E3-binding protein L3, overview	Homo sapiens	?	-	?	89	
2.3.1.12	additional information	the enzyme mediates Ca2+-activation of isozymes 1 of pyruvate dehydrogenase phosphatase by 10fold, and enhances the accessibility of the E1 substrate for the regulatory enzymes, and mediate feedback effector control by NADH and acetyl-CoA, and modifies the allosteric control, mechanism, overview	Homo sapiens	?	-	?	89	
2.3.1.12	additional information	the enzyme mediates Ca2+-activation of isozymes 1 of pyruvate dehydrogenase phosphatase by 10fold, and enhances the accessibility of the E1 substrate for the regulatory enzymes, and mediate feedback effector control by NADH and acetyl-CoA, and modifies the allosteric control, mechanism, overview	Rattus norvegicus	?	-	?	89	
2.3.1.12	additional information	interactions are different with the different isoforms of the regulatory enzymes of the multienzyme complex, signal mechanism for stimulation, overview, enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, the flexibly held outer domains of the enzyme show dynamic, E2 is responsible for effector-modified interactions with the complex' regulatory enzymes pyruvate dehydrogenase kinase PDK and pyruvate dehydrogenase phosphatase PDP, which exist in different isoforms, overview	Homo sapiens	?	-	?	89	
2.3.1.12	additional information	interactions are different with the different isoforms of the regulatory enzymes of the multienzyme complex, signal mechanism for stimulation, overview, enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, the flexibly held outer domains of the enzyme show dynamic, E2 is responsible for effector-modified interactions with the complex' regulatory enzymes pyruvate dehydrogenase kinase PDK and pyruvate dehydrogenase phosphatase PDP, which exist in different isoforms, overview	Rattus norvegicus	?	-	?	89	
2.3.1.12	additional information	the overall complex reaction is irreversible	Homo sapiens	?	-	?	89	
2.3.1.12	additional information	the overall complex reaction is irreversible	Rattus norvegicus	?	-	?	89	
2.3.1.12	additional information	Lat1 is a limiting longevity factor in nondividing cells. Overexpressing Lat1 extends cell survival during prolonged culture at stationary phase. Studies suggest that Lat1 overexpression extends life span by increasing metabolic fitness of the cell	Saccharomyces cerevisiae	?	-	?	89	
2.3.1.12	additional information	in human pyruvate dehydrogenase complex the pyruvate dehydrogenase (E1) is bound to the E1-binding domain of dihydrolipoamide acetyltransferase (E2)	Homo sapiens	?	-	?	89