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EC Tree
IUBMB 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.
The taxonomic range for the selected organisms is: Sus scrofa The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
dihydrolipoamide acetyltransferase, dihydrolipoyl transacetylase, lipoate acetyltransferase, dihydrolipoyl acetyltransferase, dhlta, dihydrolipoyl acetyl transferase, dihydrolipoyllysine-residue acetyltransferase,
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acetyltransferase, lipoate
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dihydrolipoate acetyltransferase
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dihydrolipoic transacetylase
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dihydrolipoyl acetyltransferase
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lipoate acetyltransferase
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lipoate transacetylase
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lipoic acetyltransferase
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lipoic acid acetyltransferase
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lipoic transacetylase
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lipoylacetyltransferase
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myelin-proteolipid O-palmitoyltransferase
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palmitoyl-CoA:myelin-proteolipid O-palmitoyltransferase
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thioltransacetylase A
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Acyl group transfer
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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.
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dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
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?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
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?
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dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
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?
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
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?
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brenda
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brenda
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A0A5G2QK83_PIG
638
0
68252
TrEMBL
Mitochondrion (Reliability: 2 )
A0A8D1B1A1_PIG
605
0
64476
TrEMBL
Mitochondrion (Reliability: 3 )
A0A8D1T9M2_PIG
668
0
72583
TrEMBL
Mitochondrion (Reliability: 3 )
A0A8D2A4H4_PIG
668
0
72484
TrEMBL
Mitochondrion (Reliability: 3 )
A0A8D1WF13_PIG
578
0
61800
TrEMBL
Mitochondrion (Reliability: 3 )
A0A8D0S3G8_PIG
647
0
69246
TrEMBL
Mitochondrion (Reliability: 3 )
A0A8D2BRE6_PIG
605
0
64462
TrEMBL
Mitochondrion (Reliability: 3 )
A0A5G2QFC4_PIG
520
0
55924
TrEMBL
Mitochondrion (Reliability: 3 )
K9IW70_PIG
647
0
69188
TrEMBL
Mitochondrion (Reliability: 3 )
A0A8D2AAI9_PIG
577
0
61715
TrEMBL
Mitochondrion (Reliability: 3 )
A0A8D1KHH0_PIG
542
0
57837
TrEMBL
Mitochondrion (Reliability: 3 )
A0A5G2QLQ1_PIG
647
0
69184
TrEMBL
Mitochondrion (Reliability: 3 )
A0A8D1FFV7_PIG
638
0
68256
TrEMBL
Mitochondrion (Reliability: 2 )
A0A8D0JGP7_PIG
636
0
67745
TrEMBL
Mitochondrion (Reliability: 5 )
A0A8D1KHI2_PIG
578
0
61814
TrEMBL
Mitochondrion (Reliability: 3 )
A0A5G2QIE6_PIG
541
0
57704
TrEMBL
Mitochondrion (Reliability: 3 )
Q95N04_PIG
647
0
69035
TrEMBL
Mitochondrion (Reliability: 4 )
A0A8D0J8E0_PIG
628
0
67027
TrEMBL
Mitochondrion (Reliability: 2 )
A0A8D1FIX7_PIG
520
0
55928
TrEMBL
Mitochondrion (Reliability: 3 )
A0A5G2R750_PIG
597
0
64119
TrEMBL
Mitochondrion (Reliability: 3 )
A0A5G2R3I6_PIG
667
0
71662
TrEMBL
Mitochondrion (Reliability: 3 )
A0A8D1LQ37_PIG
647
0
69287
TrEMBL
Mitochondrion (Reliability: 3 )
A0A8D1LR15_PIG
638
0
68355
TrEMBL
Mitochondrion (Reliability: 2 )
F1SMB2_PIG
578
0
61810
TrEMBL
Mitochondrion (Reliability: 3 )
A0A8D1LQ66_PIG
577
0
61814
TrEMBL
Mitochondrion (Reliability: 3 )
A0A8D0S1U9_PIG
647
0
69101
TrEMBL
Mitochondrion (Reliability: 3 )
A0A8D2BRF6_PIG
520
0
55914
TrEMBL
Mitochondrion (Reliability: 3 )
A0A4X1TBD2_PIG
647
0
69188
TrEMBL
Mitochondrion (Reliability: 3 )
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1800000 - 1970000
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calculation from sedimentation and diffusion constants, meniscus depletion method
74000
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SDS-PAGE and sedimentation equilibrium data
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polymer
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24 * 48000
polymer
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24 * 74000 SDS-PAGE, gel filtration in 6 M guanidine-HCl, sedimentation equilibrium in 6 M guanidine-HCl
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lipoprotein
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lipoprotein
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23 mol of lipoic acid per mol of enzyme
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freezing and thawing does not cause loss of activity
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-18°C, 0.05 mM potassium phosphate buffer, pH 7.0, 0.5 mM EDTA, more than 6 months
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reconstitution of pyruvate dehydrogenase complex, optimum catalytic stoichiometry of E1:E2:E3 is 5.2:11.5:2
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Yeaman, S.J.
The mammalian 2-oxoacid dehydrogenases: a complex family
Trends Biochem. Sci.
11
293-296
1986
Bos taurus, Mammalia, Sus scrofa
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brenda
Hamada, M.; Otsuka, K.I.; Tanaka, N.; Ogasahara, K.; Koike, K.; Hiraoka, T.; Koike, M.
Purification properties and subunit composition of pig heart lipoate acetyltransferase
J. Biochem.
78
187-197
1975
Sus scrofa
brenda