_EC 2.3.1.12 Dihydrolipoyllysine-residue acetyltransferase. 39 PDB entries  
EC 2.-.-.- Transferases. [17,949 PDB entries]
EC 2.3.-.- Acyltransferases. [1,204 PDB entries]
EC 2.3.1.- Transferring groups other than amino-acyl groups. [994 PDB entries]
EC 2.3.1.12 Dihydrolipoyllysine-residue acetyltransferase. [39 PDB entries]    
1b5s

Pathway: Oxo-acid dehydrogenase complexes
Reaction: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-acetyldihydrolipoyl)lysine.
 


Acetyl-CoA
+
enzyme N(6)-(dihydrolipoyl)lysine
=
CoA
+ enzyme N(6)- (S-acetyldihydrolipoyl)lysine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Acetyl-CoA:dihydrolipoamide S-acetyltransferase. Dihydrolipoamide S-acetyltransferase. Dihydrolipoate acetyltransferase. Dihydrolipoic transacetylase. Dihydrolipoyl acetyltransferase. Lipoate acetyltransferase. Lipoate transacetylase. Lipoic acetyltransferase. Lipoic acid acetyltransferase. Lipoic transacetylase.
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 and Ec 1.8.1.4. The lipoyl group of this enzyme is reductively acetylated by Ec 1.2.4.1, and the only observed direction catalyzed by Ec 2.3.1.12 is that where the acetyl group is passed to coenzyme A.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 39 PDB entries in enzyme class E.C.2.3.1.12

  PDB code Protein
1b5s
Dihydrolipoyl transacetylase (E.C.2.3.1.12) catalytic domain (residues 184-425) from bacillus stearothermophilus
Source: Geobacillus stearothermophilus. Organism_taxid: 1422
Chains: A, B, C, D, E (242 residues)
1dpb
Crystallographic and enzymatic investigations on the role of his610 and asn614 in the catalytic mechanism of azotobacter vinelandii dihydrolipoamide acetyltransferase (e2p)
Source: Azotobacter vinelandii. Organism_taxid: 354
Chain: A (243 residues) CATH domain: 3.30.559.10
1dpc
Crystallographic and enzymatic investigations on the role of his610 and asn614 in the catalytic mechanism of azotobacter vinelandii dihydrolipoamide acetyltransferase (e2p)
Source: Azotobacter vinelandii. Organism_taxid: 354
Chain: A (243 residues) CATH domain: 3.30.559.10
1dpd
Crystallographic and enzymatic investigations on the role of his610 and asn614 in the catalytic mechanism of azotobacter vinelandii dihydrolipoamide acetyltransferase (e2p)
Source: Azotobacter vinelandii. Organism_taxid: 354
Chain: A (243 residues) CATH domain: 3.30.559.10
1eaa
Atomic structure of the cubic core of the pyruvate dehydroge multienzyme complex
Source: Azotobacter vinelandii. Organism_taxid: 354
Chain: A (243 residues) CATH domain: 3.30.559.10
1eab
Atomic structure of the cubic core of the pyruvate dehydroge multienzyme complex
Source: Azotobacter vinelandii. Organism_taxid: 354
Chain: A (243 residues) CATH domain: 3.30.559.10
Bound ligands:   Het Group LPM is 92.31% similar to enzyme reactant enzyme
  Het Group COA corresponds to enzyme product CoA
1eac
Atomic structure of the cubic core of the pyruvate dehydroge multienzyme complex
Source: Azotobacter vinelandii. Organism_taxid: 354
Chain: A (243 residues) CATH domain: 3.30.559.10
Bound ligand:   Het Group CAO corresponds to enzyme product CoA
1ead
Atomic structure of the cubic core of the pyruvate dehydroge multienzyme complex
Source: Azotobacter vinelandii. Organism_taxid: 354
Chain: A (243 residues) CATH domain: 3.30.559.10
Bound ligand:   Het Group CAO is 97.96% similar to enzyme product CoA
1eae
Atomic structure of the cubic core of the pyruvate dehydroge multienzyme complex
Source: Azotobacter vinelandii. Organism_taxid: 354
Chain: A (243 residues) CATH domain: 3.30.559.10
Bound ligand:   Het Group LPM is 92.31% similar to enzyme reactant enzyme
1eaf
Atomic structure of the cubic core of the pyruvate dehydroge multienzyme complex
Source: Azotobacter vinelandii. Organism_taxid: 354
Chain: A (243 residues) CATH domain: 3.30.559.10
1ebd
Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase
Source: Geobacillus stearothermophilus. Organism_taxid: 1422. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
Chain: C (41 residues) CATH domain: 4.10.320.10
Bound ligand:   Het Group FAD is 46.00% similar to enzyme reactant acetyl-CoA
1fyc
Inner lipoyl domain from human pyruvate dehydrogenase (pdh) complex, nmr, 1 structure
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: liver. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: expressed as a gst fusion protein
Chain: A (106 residues) CATH domain: 2.40.50.100
1iyu
Lipoyl domain of pyruvate dehydrogenase complex, nmr, minimized average structure
Source: Azotobacter vinelandii. Organism_taxid: 354
Chain: A (79 residues) CATH domain: 2.40.50.100
1iyv
Lipoyl domain of pyruvate dehydrogenase complex, nmr, 29 structures
Source: Azotobacter vinelandii. Organism_taxid: 354
Chain: A (79 residues) CATH domain: 2.40.50.100
1lab
Three-dimensional structure of the lipoyl domain from bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex
Source: Geobacillus stearothermophilus. Organism_taxid: 1422. Gene: bacillus stearothermophilus.
Chain: A (80 residues) CATH domain: 2.40.50.100
1lac
Three-dimensional structure of the lipoyl domain from bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex
Source: Geobacillus stearothermophilus. Organism_taxid: 1422. Gene: bacillus stearothermophilus.
Chain: A (80 residues) CATH domain: 2.40.50.100
1qjo
Innermost lipoyl domain of the pyruvate dehydrogenase from escherichia coli
Source: Escherichia coli. Organism_taxid: 562. Strain: bl21(de3). Cellular_location: cytoplasm. Plasmid: pet11c. Gene: e2p_ecoli. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chain: A (80 residues) CATH domain: 2.40.50.100
1w3d
Nmr structure of the peripheral-subunit binding domain of bacillus stearothermophilus e2p
Source: Geobacillus stearothermophilus. Organism_taxid: 1422. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (46 residues) CATH domain: 4.10.320.10
1w4e
Peripheral-subunit binding domains from mesophilic, thermophilic, and hyperthermophilic bacteria fold by ultrafast, apparently two-state transitions
Source: Bacillus stearothermophilus. Organism_taxid: 1422. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chain: A (45 residues) CATH domain: 4.10.320.10
1w4f
Peripheral-subunit from mesophilic, thermophilic and hyperthermophilic bacteria fold by ultrafast, apparently two-state transitions
Source: Bacillus stearothermophilus. Organism_taxid: 1422. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chain: A (45 residues) CATH domain: 4.10.320.10
1w4g
Peripheral-subunit binding domains from mesophilic, thermophilic, and hyperthermophilic bacteria fold by ultrafast, apparently two-state folding transitions
Source: Bacillus stearothermophilus. Organism_taxid: 1422. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chain: A (45 residues) CATH domain: 4.10.320.10
1w85
The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2
Source: Geobacillus stearothermophilus. Organism_taxid: 1422. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
Chains: I, J (42 residues) CATH domain: 4.10.320.10
1w88
The crystal structure of pyruvate dehydrogenase e1(d180n, e183q) bound to the peripheral subunit binding domain of e2
Source: Geobacillus stearothermophilus. Organism_taxid: 1422. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
Chains: I, J (40 residues) CATH domain: 4.10.320.10
1y8n
Crystal structure of the pdk3-l2 complex
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pdk3. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693. Gene: dlat, dlta.
Chain: B (97 residues) CATH domain: 2.40.50.100
Bound ligand:   Het Group RED is 84.62% similar to enzyme reactant enzyme
1y8o
Crystal structure of the pdk3-l2 complex
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pdk3. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693. Gene: dlat, dlta.
Chain: B (97 residues) CATH domain: 2.40.50.100
Bound ligands:   Het Group RED is 84.62% similar to enzyme reactant enzyme
  Het Group ADP is 56.25% similar to enzyme product CoA
1y8p
Crystal structure of the pdk3-l2 complex
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pdk3. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693. Gene: dlat, dlta.
Chain: B (97 residues) CATH domain: 2.40.50.100
Bound ligands:   Het Group RED is 84.62% similar to enzyme reactant enzyme
  Het Group ATP is 51.92% similar to enzyme product CoA
2dne
Solution structure of rsgi ruh-058, a lipoyl domain of human 2-oxoacid dehydrogenase
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: cell free synthesis. Other_details: cell-free protein synthesis
Chain: A (108 residues) CATH domain: 2.40.50.100
2k7v
Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: acef. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (85 residues)
2pdd
The high resolution structure of the peripheral subunit- binding domain of dihydrolipoamide acetyltransferase from the pyruvate dehydrogenase multienzyme complex of bacillus stearothermophilus
Source: not given
Chain: A (43 residues) CATH domain: 4.10.320.10
2pde
The high resolution structure of the peripheral subunit-bind of dihydrolipoamide acetyltransferase from the pyruvate deh multienzyme complex of bacillus stearothermophilus
Source: not given
Chain: A (43 residues) CATH domain: 4.10.320.10
2pnr
Crystal structure of the asymmetric pdk3-l2 complex
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pdk3. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693. Gene: dlat, dlta.
Chains: C, G (79 residues) CATH domain: 2.40.50.100
Bound ligand:   Het Group RED is 84.00% similar to enzyme reactant enzyme N(6)-(dihydrolipoyl)lysine
2q8i
Pyruvate dehydrogenase kinase isoform 3 in complex with anti radicicol
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pdk3. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693. Gene: dlat, dlta.
Chain: B (93 residues) CATH domain: 2.40.50.100
Bound ligand:   Het Group RED is 84.62% similar to enzyme reactant enzyme
3b8k
Structure of the truncated human dihydrolipoyl acetyltransferase (e2)
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: dlat, dlta. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chain: A (239 residues)
3crk
Crystal structure of the pdhk2-l2 complex.
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Gene: pdk2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Homo sapiens. Human. Organism_taxid: 9606.
Chains: C, D (87 residues) CATH domain: 2.40.50.100
3crl
Crystal structure of the pdhk2-l2 complex.
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Gene: pdk2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Homo sapiens. Human. Organism_taxid: 9606.
Chains: C, D (87 residues) CATH domain: 2.40.50.100
Bound ligand:   Het Group ANP is 49.06% similar to enzyme product CoA
3duf
Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex
Source: Bacillus stearothermophilus. Gene: pdha. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: pdhb. Gene: pdhc.
Chains: I, J (38 residues)
3dv0
Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex
Source: Bacillus stearothermophilus. Gene: pdha. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: pdhb. Gene: pdhc.
Chains: I, J (43 residues) CATH domain: 4.10.320.10
3dva
Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex
Source: Bacillus stearothermophilus. Gene: pdha. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: pdhb. Gene: pdhc.
Chains: I, J (42 residues) CATH domain: 4.10.320.10
4n72
Catalytic domain from dihydrolipoamide acetyltransferase of dehydrogenase from escherichia coli
Source: Escherichia coli. Organism_taxid: 83334. Gene: acef, ecs0119, z0125. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C (246 residues) CATH domain: 3.30.559.10