2.3.1.12: dihydrolipoyllysine-residue acetyltransferase

This is an abbreviated version!
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

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

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]

General Information

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

General Information on EC 2.3.1.12 - dihydrolipoyllysine-residue acetyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide show all columns Go to General Information Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

malfunction

Homo sapiens

-

Nov3r a lipoyl group-binding site inhibitor (related trifluoro-2-hydroxy-2-menthylpropionate compound) prevents pyruvate dehydrogenase kinase2 and GST-L2 (glutathione-S-transferase fused to the inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase) binding and dissect the effects of Nov3r binding at the lipoyl group binding site on PDHK2 binding of other ligands

702229

metabolism

Homo sapiens

-

the enzyme is a mitochondrial complement component 1, q subcomponent binding protein-binding protein

735426

physiological function

4 entries

physiological function

Homo sapiens

-

in human pyruvate dehydrogenase complex the pyruvate dehydrogenase (E1) is bound to the E1-binding domain of dihydrolipoamide acetyltransferase (E2). K276 of hE2 is involved in the interaction with pyruvate dehydrogenase

686772

physiological function

Homo sapiens

P10515

structural comparison by cryo-electronmicroscopy of the human full-length and truncated dihydrolipoyl acetyltransferase cores reveal flexible linkers emanating from the edges of trimers of the internal catalytic domains. Using the secondary structure constraints revealed the 8 A cryo-electronmicroscopy and the prokaryotic truncated dihydrolipoyl acetyltransferase atomic structure as a template, a pseudo atomic model of human truncated dihydrolipoyl acetyltransferase is derived. The active sites are conserved between the truncated prokaryotic and human enzyme. Marked structural differences are apparent in the hairpin domain and in the N-terminal helix connected to the flexible linker

690088

physiological function

Homo sapiens

-

uing an in vitro reconstituted pyruvate dehydrogenase complex densitometry, isothermal titration calorimetry, and analytical ultracentrifugation evidence are provided that there are 40 copies of dihydrolipoyl transacetylase (E2p) and 20 copies of dihydrolipoamide dehydrogenase-binding protein (E3BP), in the E2p/E3BP core. The overall maximal stoichiometry of this in vitro assembled pyruvate dehydrogenase complex for dihydrolipoyl transacetylase: dihydrolipoamide dehydrogenase-binding protein: dihydrolipoamide dehydrogenase is 40:20:40:20

704473

physiological function

Chlorella sp. MM3

-

strain MM3 can grow on up to 250 microM pyrene in culture medium. With an initial cell density of 30000000 cells/ml, nearly 70% of 50 microM pyrene is degraded after 7 days of incubation, accompanied by distinct accumulation of dihydrolipoamide acetyltransferase

755757