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Literature summary for 1.2.4.4 extracted from

  • Nakai, T.; Nakagawa, N.; Maoka, N.; Masui, R.; Kuramitsu, S.; Kamiya, N.
    Ligand-induced conformational changes and a reaction intermediate in branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8, as revealed by X-ray crystallography (2004), J. Mol. Biol., 337, 1011-1033.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of alpha- and beta-subunits of component E1 in Escherichia coli Thermus thermophilus

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Inhibitors

Inhibitors Comment Organism Structure
2-chloro-4-methylpentanoate inhibits component E1, modifies a histidine side chain Thermus thermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine Thermus thermophilus
-
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
r
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

Organism

Organism UniProt Comment Textmining
Thermus thermophilus
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-
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant alpha- and beta-subunits of component E1 from Escherichia coli Thermus thermophilus

Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine
-
Thermus thermophilus [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
r
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
3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine
-
Thermus thermophilus [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
-
r
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
4-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine
-
Thermus thermophilus [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(3-methylbutanoyl)dihydrolipoyllysine + CO2
-
r
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
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 ?
-
?
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 ?
-
?

Subunits

Subunits Comment Organism
tetramer component E1, organized in alpha2beta2-structure Thermus thermophilus

Synonyms

Synonyms Comment Organism
BCOA
-
Thermus thermophilus
branched chain alpha-ketoacid dehydrogenase complex components E2 and E1 Thermus thermophilus

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate bound to complex component E1, involved in substrate recognition Thermus thermophilus