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Information on EC 2.3.1.12 - dihydrolipoyllysine-residue acetyltransferase and Organism(s) Sus scrofa

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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.
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This record set is specific for:
Sus scrofa
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Word Map
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetyltransferase, lipoate
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-
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DHLTA
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-
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dihydrolipoate acetyltransferase
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-
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dihydrolipoic transacetylase
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-
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dihydrolipoyl acetyltransferase
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-
-
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E2
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-
-
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E2p
-
-
-
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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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-
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thioltransacetylase A
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-
-
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transacetylase X
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
-
-
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 hide
9032-29-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dihydrolipoamide + acetyl-CoA
S-acetyldihydrolipoamide + CoA
show the reaction diagram
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19.7
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8 - 8.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1800000 - 1970000
-
calculation from sedimentation and diffusion constants, meniscus depletion method
48000
-
24 * 48000
74000
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SDS-PAGE and sedimentation equilibrium data
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
polymer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
stable up to
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing does not cause loss of activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, 0.05 mM potassium phosphate buffer, pH 7.0, 0.5 mM EDTA, more than 6 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of pyruvate dehydrogenase complex, optimum catalytic stoichiometry of E1:E2:E3 is 5.2:11.5:2
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yeaman, S.J.
The mammalian 2-oxoacid dehydrogenases: a complex family
Trends Biochem. Sci.
11
293-296
1986
Bos taurus, Mammalia, Sus scrofa
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team