Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dihydrolipoamide branched chain transacylase
-
-
dihydrolipoyl transacetylase
E2
-
enzyme is component of the multienzyme complex pyruvate dehydrogenase
E2p
-
E2p is a component of the human multienzyme pyruvate dehydrogenase complex
Bkd
-
-
dihydrolipoyl transacetylase
-
-
-
-
dihydrolipoyl transacetylase
-
enzyme is the E2 component of the human pyruvate dehydrogenase complex
dihydrolipoyl transacetylase
-
enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
additional information
enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
additional information
enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
additional information
enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase
additional information
enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase
additional information
-
enzyme is the E2 component of the multienzyme complex pyruvate dehydrogenase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-methylpropanoyl-CoA + dihydrolipoamide
CoA + S-2-methylpropanoyldihydrolipoamide
-
-
identification by mass spectrometry
r
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
2-oxoglutaryl-CoA + dihydrolipoamide
CoA + S-(2-oxoglutaryl)dihydrolipoamide
low activity
-
-
?
3-methylisovaleryl-CoA + dihydrolipoamide
CoA + S-(3-methylisovaleryl)dihydrolipoamide
-
-
-
?
4-methylthiobutyryl-CoA + dihydrolipoamide
CoA + S-(4-methylthiobutyryl)dihydrolipoamide
low activity
-
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
butyryl-CoA + dihydrolipoamide
CoA + S-butyryldihydrolipoamide
-
-
-
?
isobutyryl-CoA + dihydrolipoamide
CoA + S-isobutyryldihydrolipoamide
-
-
-
r
isocaproyl-CoA + dihydrolipoamide
CoA + S-isohexanoyldihydrolipoamide
-
-
-
?
isovaleryl-CoA + dihydrolipoamide
CoA + S-isovaleryldihydrolipoamide
additional information
?
-
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
-
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
-
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
-
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
-
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
-
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
-
-
r
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
recombinant apo-E2 devoid of lipoic acid is fully active
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
enzyme contains 1 lipoyl residue per E2 chain of branched-chain 2-oxo acid dehydrogenase
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
multienzyme complex, scheme of the reaction steps
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
-
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
enzyme contains 1 lipoyl residue per E2 chain of branched-chain 2-oxo acid dehydrogenase
-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
-
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
part of the pyruvate dehydrogenase reaction
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
part of the pyruvate dehydrogenase reaction
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
low activity
-
r
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
part of the pyruvate dehydrogenase reaction
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
part of the pyruvate dehydrogenase reaction
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
enzyme contains 2 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
part of the pyruvate dehydrogenase reaction
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
part of the pyruvate dehydrogenase reaction
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
part of the pyruvate dehydrogenase reaction
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
part of the pyruvate dehydrogenase reaction
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
enzyme contains 2 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
enzyme contains 3 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
part of the pyruvate dehydrogenase reaction
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
enzyme contains 1 lipoyl residue per E2 chain of pyruvate dehydrogenase complex
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
part of the pyruvate dehydrogenase reaction
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
enzyme contains 1 lipoyl residue per E2 chain of pyruvate dehydrogenase complex
-
?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
-
part of the pyruvate dehydrogenase reaction
-
?
isovaleryl-CoA + dihydrolipoamide
CoA + S-isovaleryldihydrolipoamide
-
-
-
r
isovaleryl-CoA + dihydrolipoamide
CoA + S-isovaleryldihydrolipoamide
-
recombinant enzyme, i.e. E2 domain, overexpressed in Escherichia coli
-
-
r
isovaleryl-CoA + dihydrolipoamide
CoA + S-isovaleryldihydrolipoamide
-
-
-
?
additional information
?
-
-
enzyme is a mitochondrial autoantigen, epitope mapping is performed to define the recognition sites by sera and T cells of patients suffering idopathic dilated cardiomyopathy and dilated cardiomyopathy
-
-
?
additional information
?
-
pyruvate is a poor substrate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
24-mer
-
24 * 52000, SDS-PAGE
?
-
x * 52600, SDS-PAGE
additional information
-
lipoyl domains and inner core in the structure of multienzyme complex, overview
additional information
-
C-terminus of E2 is joined to the N-terminus of E3 in the pyruvate dehydrogenase complex, subunit organization
additional information
-
lipoyl domains and inner core in the structure of multienzyme complex, overview
additional information
-
recombinant apo-E2 is unable to reconstitute with recombinant E1 and E3 to an active branched-chain alpha-keto dehydrogenase, but recombinant holo-E2 is able to
additional information
-
in vitro reconstitution of the 24-meric E2 inner core requires the chaperonins GroEL and GroES
additional information
-
subunit structure analysis by tryptic digest
additional information
-
the 24-mer can be separated into active trimers of MW 84 kDa by incubation in 1.5 M guanidinium-HCl at 25°C, process is reversible, and removal of guanidinium-HCl leads to spontenaous reassembly to an active 24-mer
additional information
-
enzyme shows the E2 structure of 3 folded domains: lipoyl-bearing, E3-binding, and inner core, typical for all E2 protein of alpha-keto acid dehydrogenases
additional information
-
lipoate-free inner E2 core: 26 kDa fragment contains the active site, 22 kDa fragment B is the subunit-binding domain, fragments are gained by tryptic digest
additional information
-
the 26 kDa fragment from tryptic digest is the catalytically active part of the enzyme
additional information
-
assembly of 24 E2 subunits into a cubic structure, forming the core of the mammalian branched-chain alpha-keto acid dehydrogenase multienzyme complex
additional information
-
lipoyl domains and inner core in the structure of multienzyme complex, overview
additional information
-
lipoyl domains and inner core in the structure of multienzyme complex, overview
additional information
-
lipoyl domains and inner core in the structure of multienzyme complex, overview
additional information
-
lipoyl domains and inner core in the structure of multienzyme complex, overview
additional information
assembly of 24 E2 subunits into a cubic structure, forming the core of the mammalian branched-chain alpha-keto acid dehydrogenase multienzyme complex
additional information
-
The human pyruvate dehydrogenase complex (PDC) is organized around a 60-meric dodecahedral core comprising the C-terminal domains of E2p and a noncatalytic component, E3-binding protein (E3BP), which specifically tethers E3 dimers to the PDC. Using an in vitro reconstituted PDC, densitometry, isothermal titration calorimetry, and analytical ultracentrifugation evidence provide that there are 40 copies of E2p and 20 copies of E3BP in the E2p/E3BP core. The overall maximal stoichiometry of this in vitro assembled PDC for E2p:E3BP:E1p:E3 is 40:20:40:20.
additional information
reconstitution of the multienzyme complex branched-chain alpha-keto dehydrogenase
additional information
-
lipoyl domains and inner core in the structure of multienzyme complex, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Chuang, D.T.; Hu, C.C.; Ku, L.S.; Niu, W.L.; Myers, D.E.; Cox, R.P.
Catalytic and structural properties of the dihydrolipoyl transacylase component of bovine branched-chain alpha-keto acid dehydrogenase
J. Biol. Chem.
259
9277-9284
1984
Bos taurus
brenda
Chuang, D.T.; Hu, C.W.; Ku, L.S.; Markovitz, P.J.; Cox, R.P.
Subunit structure of the dihydrolipoyl transacylase component of branched-chain alpha-keto acid dehydrogenase complex from bovine liver. Characterization of the inner transacylase core
J. Biol. Chem.
260
13779-13786
1985
Bos taurus
brenda
Hu, C.W.; Griffin, T.A.; Lau, K.S.; Cox, R.P.; Chuang, D.T.
Subunit structure of the dihydrolipoyl transacylase component of branched-chain alpha-keto acid dehydrogenase complex from bovine liver. Mapping of the lipoyl-bearing domain by limited proteolysis
J. Biol. Chem.
261
343-349
1986
Bos taurus
brenda
Chuang, D.T.; Fisher, C.W.; Lau, K.S.; Griffin, T.A.; Wynn, R.M.; Cox, R.P.
Maple syrup urine disease: domain structure, mutations and exon skipping in the dihydrolipoyl transacylase (E2) component of the branched-chain alpha-keto acid dehydrogenase complex
Mol. Biol. Med.
8
49-63
1991
Bos taurus, Homo sapiens (P11182)
brenda
Lau, K.S.; Herring, W.J.; Chuang, J.L.; McKean, M.; Danner, D.J.; Cox, R.P.; Chuang, D.T.
Structure of the gene encoding dihydrolipoyl transacylase (E2) component of human branched chain alpha-keto acid dehydrogenase complex and characterization of an E2 pseudogene
J. Biol. Chem.
267
24090-24096
1992
Homo sapiens (P11182)
brenda
Lau, K.S.; Chuang, J.L.; Herring, W.J.; Danner, D.J.; Cox, R.P.; Chuang, D.T.
The complete cDNA sequence for dihydrolipoyl transacylase (E2) of human branched-chain alpha-keto acid dehydrogenase complex
Biochim. Biophys. Acta
1132
319-321
1992
Homo sapiens (P11182)
brenda
Ansari, A.A.; Neckelmann, N.; Villinger, F.; Leung, P.; Danner, D.J.; Brar, S.S.; Zhao, S.; Gravanis, M.B.; Mayne, A.; Gershwin, M.E.
Epitope mapping of the branched chain alpha-ketoacid dehydrogenase dihydrolipoyl transacylase (BCKD-E2) protein that reacts with sera from patients with idiopathic dilated cardiomyopathy
J. Immunol.
153
4754-4765
1994
Bos taurus, Homo sapiens
brenda
Perham, R.N.
Swinging arms and swinging domains in multifunctional emzymes: catalytic machines for multistep reactions
Annu. Rev. Biochem.
69
961-1004
2000
Azotobacter vinelandii, Acidithiobacillus ferrooxidans, Cupriavidus necator, Geobacillus stearothermophilus, Saccharomyces cerevisiae, Escherichia coli, Enterococcus faecalis, Haemophilus influenzae, Homo sapiens, Neisseria meningitidis, no activity in archaebacteria, no activity in Desulfovibrio africanus, Zymomonas mobilis
brenda
Chuang, J.L.; Davie, J.R.; Wynn, R.M.; Chuang, D.T.
Production of recombinant mammalian holo-E2 and E3 and reconstitution of functional branched-chain alpha-keto acid dehydrogenase complex with recombinant E1
Methods Enzymol.
324
192-200
2000
Bos taurus
brenda
Hakozaki, M.; Ono, K.; Suzuki, T.; Hata, H.; Mori, T.; Kochi, H.
Characterization of rainbow trout branched-chain alpha-keto acid dehydrogenase complex: inter-domain segments of the E2 component affect the overall activity
Comp. Biochem. Physiol. B Biochem. Mol. Biol.
132
433-442
2002
Oncorhynchus mykiss (Q8QHL7), Gallus gallus (Q98UJ6)
brenda
Wynn, R.M.; Davie, J.R.; Zhi, W.; Cox, R.P.; Chuang, D.T.
Invitro reconstitution of the 24-meric E2 inner core of bovine mitochondrial branched-chain alpha-keto acid dehydrogenase complex: requirements for chaperonins GroEL and GroES
Biochemistry
33
8962-8968
1994
Bos taurus
brenda
Klyuyeva, A.; Tuganova, A.; Popov, K.M.
Allosteric coupling in pyruvate dehydrogenase kinase 2
Biochemistry
47
8358-8366
2008
Rattus norvegicus
brenda
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
brenda
Cui, Q.; Zhou, F.; Liu, W.; Tao, Y.
Avermectin biosynthesis stable functional expression of branched chain alpha-keto acid dehydrogenase complex from Streptomyces avermitilis in Escherichia coli by selectively regulating individual subunit gene expression
Biotechnol. Lett.
39
1567-1574
2017
Streptomyces avermitilis
brenda
Tsai, H.Y.; Wu, S.C.; Li, J.C.; Chen, Y.M.; Chan, C.C.; Chen, C.H.
Loss of the Drosophila branched-chain alpha-keto acid dehydrogenase complex (BCKDH) results in neuronal dysfunction
Dis. Model. Mech.
13
dmm044750
2020
Drosophila melanogaster
brenda
Usman, B.; Nawaz, G.; Zhao, N.; Liao, S.; Qin, B.; Liu, F.; Liu, Y.; Li, R.
Programmed editing of rice ( Oryza sativa L.) OsSPL16 gene using CRISPR/Cas9 improves grain yield by modulating the expression of pyruvate enzymes and cell cycle proteins
Int. J. Mol. Sci.
22
249
2020
Oryza sativa Indica Group
brenda
Singh, V.K.; Sirobhushanam, S.; Ring, R.P.; Singh, S.; Gatto, C.; Wilkinson, B.J.
Roles of pyruvate dehydrogenase and branched-chain alpha-keto acid dehydrogenase in branched-chain membrane fatty acid levels and associated functions in Staphylococcus aureus
J. Med. Microbiol.
67
570-578
2018
Staphylococcus aureus, Staphylococcus aureus JE2
brenda
Hull, J.; Usmari Moraes, M.; Brookes, E.; Love, S.; Conway, M.
Distribution of the branched-chain alpha-ketoacid dehydrogenase complex E1alpha subunit and glutamate dehydrogenase in the human brain and their role in neuro-metabolism
Neurochem. Int.
112
49-58
2018
Homo sapiens (P09622)
brenda