2.3.1.12: dihydrolipoyllysine-residue acetyltransferase

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For detailed information about dihydrolipoyllysine-residue acetyltransferase, go to the full flat file.

Reaction

Synonyms

acetyltransferase, lipoate, DHLTA, dihydrolipoamide acetyltransferase, dihydrolipoate acetyltransferase, dihydrolipoic transacetylase, dihydrolipoyl acetyl transferase, dihydrolipoyl acetyltransferase, dihydrolipoyl acetyltransferase component E2, dihydrolipoyl acetyltransferase E2p, dihydrolipoyl transacetylase, dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial, DLAT, E2, E2p, hE2, Lat1, lipoate acetyltransferase, lipoate transacetylase, lipoic acetyltransferase, lipoic acid acetyltransferase, lipoic transacetylase, lipoylacetyltransferase, More, myelin-proteolipid O-palmitoyltransferase, palmitoyl-CoA:myelin-proteolipid O-palmitoyltransferase, pyruvate dehydrogenase complex component E2, pyruvate dehydrogenase complex component E2p, pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase component, thioltransacetylase A, transacetylase X

ECTree

     2 Transferases

         2.3 Acyltransferases

             2.3.1 Transferring groups other than aminoacyl groups

                2.3.1.12 dihydrolipoyllysine-residue acetyltransferase

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Results	in table
20867	AA Sequence
2	Application
1	CAS Registry Number
35	Cloned(Commentary)
1	Cofactor
8	Crystallization (Commentary)
84	Disease/ Diagnostics
6	General Information
3	General Stability
10	Inhibitors
20	KM Value [mM]
18	Localization
7	Metals/Ions
95	Molecular Weight [Da]
93	Natural Substrates/ Products (Substrates)
108	Organism
10	Pathway
269	PDB ID
4	pH Optimum
2	pH Stability
19	Posttranslational Modification
62	Protein Variants
62	Purification (Commentary)
3	Reaction
1	Reaction Type
107	Reference
13	Renatured (Commentary)
37	Source Tissue
17	Specific Activity [micromol/min/mg]
2	Storage Stability
100	Substrates and Products (Substrate)
60	Subunits
63	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
5	Temperature Stability [°C]
4	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.3.1.12 - dihydrolipoyllysine-residue acetyltransferase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

hanging drop vapor diffusion method

Azotobacter vinelandii

-

486228, 486236

pyruvate dehydrogenase complex

Bos taurus

-

94893

E1p-E2p didomain subcomplex, sitting drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.2% (w/v) NaN3, and 0.2 M ammonium tartrate dibasic buffer (pH 6.35)

Escherichia coli

P06959

736459

E2-E3 subcomplex of pyruvate dehydrogenase, E2: EC 2.3.1.12, E3: EC 1.8.1.4, various crystallization conditions

Escherichia coli

-

486199

His9-tagged catalytic domain, hanging drop vapor diffusion method, using 0.2 M potassium thiocyanate and 20% (w/v) polyethylene glycol 3350

Escherichia coli

P06959

736448

E3 dimer with E2 and a small binding domain E2BD, hanging drop vapor diffusion method

Geobacillus stearothermophilus

-

486230

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

Homo sapiens

-

704423