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Literature summary for 6.3.2.26 extracted from

  • Coque, J.J.R.; De la Fuente, J.L.; Liras, P.; Martin, J.F.
    Overexpression of the Nocardia lactamdurans alpha-aminoadipyl-cysteinyl-valine synthetase in Streptomyces lividans. The purified multienzyme uses cystathionine and 6-oxopiperidine 2-carboxylate as substrates for synthesis of the tripeptide (1996), Eur. J. Biochem., 242, 264-270.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Streptomyces lividans Amycolatopsis lactamdurans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
430000
-
gel filtration Amycolatopsis lactamdurans

Organism

Organism UniProt Comment Textmining
Amycolatopsis lactamdurans
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Amycolatopsis lactamdurans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
55.71
-
-
Amycolatopsis lactamdurans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6-oxopiperidine 2-carboxylic acid + L-cysteine + L-valine + ATP
-
Amycolatopsis lactamdurans N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
-
?
L-2-aminoadipate + L-cystathionine + L-valine + ATP
-
Amycolatopsis lactamdurans N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
-
?
L-2-aminoadipate + L-cysteine + L-valine + ATP
-
Amycolatopsis lactamdurans N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
-
?

Subunits

Subunits Comment Organism
monomer 1 * 430000, SDS-PAGE Amycolatopsis lactamdurans

Cofactor

Cofactor Comment Organism Structure
ATP
-
Amycolatopsis lactamdurans