EC Number | Cloned (Comment) | Organism |
---|---|---|
1.2.4.4 | expression of alpha- and beta-subunits of component E1 in Escherichia coli | Thermus thermophilus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.2.4.4 | crystallization of 4 forms of complex component E1: 1. E1 apoenzyme, 2. E1 holoenzyme, 3. E1 holoenzyme in complex with substrate analogue 4-methylpentanoate, 4. E1 holoenzyme in complex with substrate 4-methyl-2-oxopentanoate, hanging drop vapour diffusion method, 18°C, 0.002 ml 10 mg/ml purified recombinant protein in 20 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1 mM DTT, with equal volume of 0.002 ml of reservoir solution containing 0.7 M lithium sulfate, 60 mM sodium citrate, pH 5.6, against 0.4 ml reservoir solution, a few days, X-ray diffraction structure determination and analysis at 1.9-2.4 A resolution | Thermus thermophilus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.2.4.4 | 2-chloro-4-methylpentanoate | inhibits component E1, modifies a histidine side chain | Thermus thermophilus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.2.4.4 | Mg2+ | required | Thermus thermophilus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.4.4 | 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine | Thermus thermophilus | - |
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2 | - |
r | |
1.2.4.4 | 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | - |
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2 | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.2.4.4 | Thermus thermophilus | - |
- |
- |
1.2.4.4 | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.2.4.4 | recombinant alpha- and beta-subunits of component E1 from Escherichia coli | Thermus thermophilus |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.2.4.4 | 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2 + 2 H+ | substrate recognition and reaction mechanism, involving residues Gly131beta-Gln131beta, Phe66alpha, Tyr86beta, Tyr95alpha, Met128alpha, His131alpha of component E1 | Thermus thermophilus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.4.4 | 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine | - |
Thermus thermophilus | [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2 | - |
r | |
1.2.4.4 | 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2 | - |
r | |
1.2.4.4 | 3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine | - |
Thermus thermophilus | [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2 | - |
r | |
1.2.4.4 | 3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2 | - |
r | |
1.2.4.4 | 4-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine | - |
Thermus thermophilus | [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(3-methylbutanoyl)dihydrolipoyllysine + CO2 | - |
r | |
1.2.4.4 | 4-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(3-methylbutanoyl)dihydrolipoyllysine + CO2 | - |
r | |
1.2.4.4 | additional information | decarboxylation and acylation reaction proceeds in 4 reaction steps in the enzyme complex, involving the cofactor thiamine diphosphate and the lipoic acid-bearing domain of component E2, E1 undergoes an open-closed conformational change upon formation of the enzyme-substrate complex, overview | Thermus thermophilus | ? | - |
? | |
1.2.4.4 | additional information | decarboxylation and acylation reaction proceeds in 4 reaction steps in the enzyme complex, involving the cofactor thiamine diphosphate and the lipoic acid-bearing domain of component E2, E1 undergoes an open-closed conformational change upon formation of the enzyme-substrate complex, overview | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.2.4.4 | tetramer | component E1, organized in alpha2beta2-structure | Thermus thermophilus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.2.4.4 | BCOA | - |
Thermus thermophilus |
1.2.4.4 | branched chain alpha-ketoacid dehydrogenase complex | components E2 and E1 | Thermus thermophilus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.2.4.4 | thiamine diphosphate | bound to complex component E1, involved in substrate recognition | Thermus thermophilus |