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Information on EC 2.3.1.12 - dihydrolipoyllysine-residue acetyltransferase and Organism(s) Homo sapiens and UniProt Accession P10515
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2.3.1.12 dihydrolipoyllysine-residue acetyltransferaseIUBMB Comments
A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC 1.2.4.1, pyruvate dehydrogenase (acetyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalysed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A.
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Word Map
- 2.3.1.12
-
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
-
e1beta
-
2-14cpyruvate
- molecular biology
- degradation
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
dihydrolipoamide acetyltransferase, dihydrolipoyl transacetylase, lipoate acetyltransferase, dihydrolipoyl acetyltransferase, dhlta, dihydrolipoyl acetyl transferase, dihydrolipoyllysine-residue acetyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyltransferase, lipoate
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-
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DHLTA
-
-
-
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dihydrolipoate acetyltransferase
-
-
-
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dihydrolipoic transacetylase
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-
-
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dihydrolipoyl acetyltransferase
dihydrolipoyl transacetylase
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
-
-
E2
E2p
lipoate acetyltransferase
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-
-
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lipoate transacetylase
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-
-
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lipoic acetyltransferase
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-
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lipoic acid acetyltransferase
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-
-
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lipoic transacetylase
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-
-
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lipoylacetyltransferase
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-
-
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myelin-proteolipid O-palmitoyltransferase
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-
-
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palmitoyl-CoA:myelin-proteolipid O-palmitoyltransferase
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thioltransacetylase A
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-
-
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transacetylase X
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-
-
-
additional information
dihydrolipoyl acetyltransferase
-
-
-
-
dihydrolipoyl acetyltransferase
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glutathione-S-transferase fused to the inner lipoyl domain is used
dihydrolipoyl transacetylase
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is part of the human pyruvate dehydrogenase complex
E2
-
-
-
-
E2p
-
-
-
-
additional information
-
the enzyme forms the core unit E2 of the pyruvate dehydrogenase multienzyme complex binding the other components, i.e. pyruvate decarboxylase E1 and dihydrolipoyl dehydrogenase E3, tightly at its innerlipoyl or N-terminal lipoyl domain, respectively, composition overview
additional information
-
the enzyme forms the core unit E2 of the pyruvate dehydrogenase multienzyme complex binding the other components, i.e. pyruvate decarboxylase E1 and dihydrolipoyl dehydrogenase E3, tightly at its innerlipoyl or N-terminal lipoyl domain, respectively, composition overview
additional information
-
the enzyme is a subunit of the pyruvate dehydrogenase multienzyme complex, the enzyme forms the core unit E2 of the pyruvate dehydrogenase multienzyme complex binding the other components, i.e. pyruvate decarboxylase E1 and dihydrolipoyl dehydrogenase E3, tightly at its innerlipoyl or N-terminal lipoyl domain, respectively, composition overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:enzyme N6-(dihydrolipoyl)lysine S-acetyltransferase
A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC 1.2.4.1, pyruvate dehydrogenase (acetyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalysed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A.
CAS REGISTRY NUMBER
COMMENTARY
9032-29-5
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SUBSTRATE
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
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-
-
-
?
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
-
-
?
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
-
-
?
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
?
-
-
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
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-
?
additional information
?
-
-
in human pyruvate dehydrogenase complex the pyruvate dehydrogenase (E1) is bound to the E1-binding domain of dihydrolipoamide acetyltransferase (E2)
-
-
?
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
-
-
-
-
?
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
-
-
?
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
-
-
?
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
?
-
-
in human pyruvate dehydrogenase complex the pyruvate dehydrogenase (E1) is bound to the E1-binding domain of dihydrolipoamide acetyltransferase (E2)
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
-
association of the pyruvate dehydrogenase kinase2 and GST-L2 (glutathione-S-transferase fused to the inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase (E2)) dimers is enhanced by K+
phosphate
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phosphate has a pronounced effect in increasing ligand interference with pyruvate dehydrogenase kinase2 and GST-L2 (glutathione-S-transferase fused to the inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase (E2))
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
guanidine hydrochloride
-
50% inhibition at 0.3 M, complete inhibition at 0.7-1 M
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
binding constants of multienzyme complex components and regulatory enzymes, overview
-
additional information
additional information
-
complex component interactions among each other and with regulatory enzyme pyruvate dehydrogenase kinase isozyme 2, overview, dissociation constants of interaction of L2 and recombinant GST-L2 with PDK isozyme 2, reduced PDK2 binding to E2-E1, reversible bifunctional binding to L2 with the mandatory singly held transition fits the proposed 'hand-over-hand' movement of a kinase dimer to access E1 without dissociating from the complex
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
structural comparison by cryo-electronmicroscopy of the human full-length and truncated dihydrolipoyl acetyltransferase cores reveal flexible linkers emanating from the edges of trimers of the internal catalytic domains. Using the secondary structure constraints revealed the 8 A cryo-electronmicroscopy and the prokaryotic truncated dihydrolipoyl acetyltransferase atomic structure as a template, a pseudo atomic model of human truncated dihydrolipoyl acetyltransferase is derived. The active sites are conserved between the truncated prokaryotic and human enzyme. Marked structural differences are apparent in the hairpin domain and in the N-terminal helix connected to the flexible linker
malfunction
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Nov3r a lipoyl group-binding site inhibitor (related trifluoro-2-hydroxy-2-menthylpropionate compound) prevents pyruvate dehydrogenase kinase2 and GST-L2 (glutathione-S-transferase fused to the inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase) binding and dissect the effects of Nov3r binding at the lipoyl group binding site on PDHK2 binding of other ligands
metabolism
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the enzyme is a mitochondrial complement component 1, q subcomponent binding protein-binding protein
physiological function
physiological function
-
in human pyruvate dehydrogenase complex the pyruvate dehydrogenase (E1) is bound to the E1-binding domain of dihydrolipoamide acetyltransferase (E2). K276 of hE2 is involved in the interaction with pyruvate dehydrogenase
physiological function
-
uing an in vitro reconstituted pyruvate dehydrogenase complex densitometry, isothermal titration calorimetry, and analytical ultracentrifugation evidence are provided that there are 40 copies of dihydrolipoyl transacetylase (E2p) and 20 copies of dihydrolipoamide dehydrogenase-binding protein (E3BP), in the E2p/E3BP core. The overall maximal stoichiometry of this in vitro assembled pyruvate dehydrogenase complex for dihydrolipoyl transacetylase: dihydrolipoamide dehydrogenase-binding protein: dihydrolipoamide dehydrogenase is 40:20:40:20
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ODP2_HUMAN
647
0
68997
Swiss-Prot
Mitochondrion (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
200000
-
at 1.8 - 2.8 M guanidine hydrochloride, complex dissociates at higher guanidine hydrochloride levels to a monomeric form with MW 82000
82000
-
3 * 82000, gel filtration, trimeric form occurs in solutions with 4 M guanidine hydrochloride
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
trimer
-
3 * 82000, gel filtration, trimeric form occurs in solutions with 4 M guanidine hydrochloride
additional information
dimer
-
GST-L2, glutathione-S-transferase fused to the inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase exists as a dimer
additional information
evidence for a novel subunit organization in which dihydrolipoamide dehydrogenase E3 and E3BP form subcomplexes with a 1:2 stoichiometry implying the existence of a network of dihydrolipoamide dehydrogenase cross-bridges linking pairs of E3-binding proteins across the surface of the dihydrolipoamide acetyltransferase E2 core assembly. One of the E3-binding protein lipoyl domains docks into the dihydrolipoamide dehydrogenase E3 active site
additional information
-
E2 is composed of 4 domains including the innerlipoyl domain L2 important for binding of E1
additional information
-
enzyme is a 60mer, E2 domain structure: 4 domains, i.e. L1, L2, B, and I domain, connected by linker oligomers, overview, overall multienzyme complex organization, overview
additional information
-
the enzyme forms the core unit E2, consisting of 4 domains in 60mer, a trimer of 3 20mers, of the pyruvate dehydrogenase multienzyme complex binding the other components, i.e. pyruvate decarboxylase and dihydrolipoyl dehydrogenase, tightly at its innerlipoyl or N-terminal lipoyl domain, respectively, composition overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of pyruvate dehydrogenase kinase 2 bound to the inner lipoyl-bearing domain of dihydrolipoamide transacetylase is determined. Crystal structure reveals a pyruvate dehydrogenase kinase 2 dimer complexed with two inner lipoyl-bearing domains of dihydrolipoamide transacetylase. Comparison with apo-pyruvate dehydrogenase kinase 2 shows that dihydrolipoamide transacetylase binding causes rearrangements in PDHK2 structure that affect the dihydrolipoamidetransacetylase- and pyruvate dehydrogenase-binding sites
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A174S
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: 69%
D164A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: 55%
D172A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: 66%
E162A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: 93%
E179A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: 28%
E182A
E182Q
-
binding of mutant L2 domain to pyruvate dehydrogenase phosphatase isozyme 1 is hindered
E183A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: 98%
I176A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: not measurable
I229A/F231A
-
ability to be post-translationally lipoylated remains, far-UV CD spectrum differs from wild-type enzyme
K173A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: not measurable
K276A
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mutant shows negligible binding to human pyruvate dehydrogenase with 86fold higher KD compared to wild-type
L140A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: not measurable
R196A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: 79%
R297A
-
mutant is found to have KD 6.8fold higher than that for the wild-type, indicating a possible involvement of this residue in the interaction with human pyruvate dehydrogenase, but not with the C-terminal residue of beta-subunit
V180S/E181L
-
binding of mutant L2 domain to pyruvate dehydrogenase phosphatase isozyme 1 is hindered
V188A
-
ability to be post-translationally lipoylated remains, far-UV CD spectrum differs from wild-type enzyme
additional information
E182A
-
binding of mutant L2 domain to pyruvate dehydrogenase phosphatase isozyme 1 is hindered
E182A
-
mutation in the inner lipoyl-bearing domain (L2), pyruvate dehydrogenase kinase 2 binding: 100%
additional information
a truncated version of dihydrolipoyl acetyltransferase is created lacking the N-terminal 319 amino acids
additional information
-
a truncated version of dihydrolipoyl acetyltransferase is created lacking the N-terminal 319 amino acids
additional information
-
construction of diverse L2 domain mutants, e.g. substitutions of A172, D173, Leu140, Glu162, Glu181, and Glu179 highly reduce binding of L2 domain to pyruvate dehydrogenase phosphatase isozyme 1
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a recombinant fragment hL2S (containing the second lipoyl domain (L2), second hinge region, E1-binding domain (S) and third hinge region of hE2, residues 128330) is overexpressed in Escherichia coli
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inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase is expressed as a GST fusion protein
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the inner lipoyl-bearing domain of dihydrolipoamide transacetylase is expressed as a GST fusion protein in Escherichia coli
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
treatment with guanidine hydrochloride and its subsequent removal results in refolding
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Thekkumkara, T.J.; Jesse, B.W.; Ho, L.; Raefsky, C.; Pepin, R.A.; Javed, A.A.; Pons, G.; Patel, M.S.
Isolation of a cDNA clone for the dihydrolipoamide acetyltransferase component of the human liver pyruvate dehydrogenase complex
Biochem. Biophys. Res. Commun.
145
903-907
1987
Homo sapiens
Jackson, J.C.; Vinluan, C.C.; Dragland, C.J.; Sundararajan, V.; Yan, B.; Gounarides, J.S.; Nirmala, N.R.; Topiol, S.; Ramage, P.; Blume, J.E.; Aicher, T.D.; Bell, P.A.; Mann, W.R.
Heterologously expressed inner lipoyl domain of dihydrolipoyl acetyltransferase inhibits ATP-dependent inactivation of pyruvate dehydrogenase complex, Identification of important amino acid residues
Biochem. J.
334
703-711
1998
Homo sapiens
-
McCartney, R.G.; Sanderson, S.J.; Lindsay, J.G.
Refolding and reconstitution studies on the transacetylase-protein X (E2/X) subcomplex of the mammalian pyruvate dehydrogenase complex: Evidence for specific binding of the dihydrolipoamide dehydrogenase component to sites on reassembled E2
Biochemistry
36
6819-6826
1997
Homo sapiens
Yang, D.; Song, J.; Wagenknecht, T.; Roche, T.E.
Assembly and full functionality of recombinantly expressed dihydrolipoyl acetyltransferase component of the human pyruvate dehydrogenase complex
J. Biol. Chem.
272
6361-6369
1997
Homo sapiens
Roche, T.E.; Hiromasa, Y.; Turkan, A.; Gong, X.; Peng, T.; Yan, X.; Kasten, S.A.; Bao, H.; Dong, J.
Essential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1
Eur. J. Biochem.
270
1050-1056
2003
Homo sapiens, Rattus norvegicus
Hiromasa, Y.; Roche, T.E.
Facilitated interaction between the pyruvate dehydrogenase kinase isoform 2 and the dihydrolipoyl acetyltransferase
J. Biol. Chem.
278
33681-33693
2003
Homo sapiens
Roche, T.E.; Hiromasa, Y.; Turkan, A.; Gong, X.; Peng, T.; Yan, X.; Kasten, S.A.; Bao, H.; Dong, J.
Central organization of mammalian pyruvate dehydrogenase (PD) complex and lipoyl domain-mediated activated function and control of PD kinases and phosphatase 1
Oxid. Stress Dis.
11
363-386
2004
Homo sapiens, Rattus norvegicus
-
Tuganova, A.; Klyuyeva, A.; Popov, K.M.
Recognition of the inner lipoyl-bearing domain of dihydrolipoyl transacetylase and of the blood glucose-lowering compound AZD7545 by pyruvate dehydrogenase kinase 2
Biochemistry
46
8592-8602
2007
Homo sapiens
Hiromasa, Y.; Hu, L.; Roche, T.E.
Ligand-induced effects on pyruvate dehydrogenase kinase isoform 2
J. Biol. Chem.
281
12568-12579
2006
Homo sapiens
Smolle, M.; Prior, A.E.; Brown, A.E.; Cooper, A.; Byron, O.; Lindsay, J.G.
A new level of architectural complexity in the human pyruvate dehydrogenase complex
J. Biol. Chem.
281
19772-19780
2006
Homo sapiens (P10515)
Korotchkina, L.G.; Patel, M.S.
Binding of pyruvate dehydrogenase to the core of the human pyruvate dehydrogenase complex
FEBS Lett.
582
468-472
2008
Homo sapiens
Yu, X.; Hiromasa, Y.; Tsen, H.; Stoops, J.K.; Roche, T.E.; Zhou, Z.H.
Structures of the human pyruvate dehydrogenase complex cores: a highly conserved catalytic center with flexible N-terminal domains
Structure
16
104-114
2008
Homo sapiens (P10515), Homo sapiens
Hiromasa, Y.; Yan, X.; Roche, T.E.
Specific ion influences on self-association of pyruvate dehydrogenase kinase isoform 2 (PDHK2), binding of PDHK2 to the L2 lipoyl domain, and effects of the lipoyl group-binding site inhibitor, Nov3r
Biochemistry
47
2312-2324
2008
Homo sapiens
Green, T.; Grigorian, A.; Klyuyeva, A.; Tuganova, A.; Luo, M.; Popov, K.
Structural and functional insights into the molecular mechanisms responsible for the regulation of pyruvate dehydrogenase kinase 2
J. Biol. Chem.
283
15789-15798
2008
Homo sapiens
Brautigam, C.A.; Wynn, R.M.; Chuang, J.L.; Chuang, D.T.
Subunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex
J. Biol. Chem.
284
13086-13098
2009
Homo sapiens
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