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
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2.3.1.12
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lipoylated
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multienzyme
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stearothermophilus
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thiamin
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azotobacter
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vinelandii
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subcomplexes
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subunit-binding
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lipoyl-lysine
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e3-binding
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icosahedral
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pdc-e2
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1.2.4.1
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lipoyl-bearing
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dodecahedron
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alpha2beta2
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pentagonal
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e1alpha
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e1beta
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2-14cpyruvate
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molecular biology
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degradation
- 2.3.1.12
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lipoylated
-
multienzyme
- stearothermophilus
- thiamin
-
azotobacter
- vinelandii
-
subcomplexes
-
subunit-binding
-
lipoyl-lysine
-
e3-binding
-
icosahedral
- pdc-e2
-
1.2.4.1
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lipoyl-bearing
-
dodecahedron
-
alpha2beta2
-
pentagonal
- e1alpha
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e1beta
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2-14cpyruvate
- molecular biology
- degradation
Reaction
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
2.3.1.12 dihydrolipoyllysine-residue acetyltransferaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 2.3.1.12 - dihydrolipoyllysine-residue acetyltransferase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine
acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine
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-
-
?
acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine
-
-
-
r
acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine
-
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
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acetyl group is transferred from the S-acetyldihydrolipoyl moiety bound covalently to the transacetylase to CoA
-
r
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
-
-
-
?
additional information
?
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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
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-
?
additional information
?
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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
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?
additional information
?
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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
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-
?
additional information
?
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in human pyruvate dehydrogenase complex the pyruvate dehydrogenase (E1) is bound to the E1-binding domain of dihydrolipoamide acetyltransferase (E2)
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-
?
additional information
?
-
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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
-
-
?
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
-
-
?
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
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-
?
additional information
?
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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
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-
?
additional information
?
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protein bound acetyldihydrolipoyl moiety + CoA
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-
?
