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Literature summary for 1.5.1.24 extracted from

  • Miller, S.P.F.; Donkersloot, J.A.; Thompson, J.
    Enzymatic synthesis and characterization of N5-(carboxymethyl)-L-ornithine and N6-(carboxymethyl)-L-lysine (1994), Amino Acids, 6, 189-198.
    View publication on PubMed

Application

Application Comment Organism
synthesis enzymatic biosyntheses of amino acids instead of chemical syntheses provide an attractive alternative to the former procedures since they are efficient and simple to perform. N,N-dialkylation does not occur and the enzyme-catalyzed reactions are both regio-and stereochemically specific Lactococcus lactis

Cloned(Commentary)

Cloned (Comment) Organism
gene ceo, encoding the tetrameric enzyme, cloned and sequenced, plasmid p493 containing ceo transformed into Escherichia coli TG1 Lactococcus lactis

Inhibitors

Inhibitors Comment Organism Structure
gamma-glutamyl peptide
-
Lactococcus lactis
additional information anti-NADP+ oxidoreductase IgG Lactococcus lactis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.15
-
pyruvate
-
Lactococcus lactis

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Lactococcus lactis 5737
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35323
-
4 * 35323, deduced from amino acid sequence Lactococcus lactis

Organism

Organism UniProt Comment Textmining
Lactococcus lactis
-
subsp. lactis
-

Purification (Commentary)

Purification (Comment) Organism
-
Lactococcus lactis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
lysine + pyruvate + NADPH
-
Lactococcus lactis N7-(1-carboxyethyl)lysine + NADP+ + H2O
-
ir

Subunits

Subunits Comment Organism
tetramer 4 * 35323, deduced from amino acid sequence Lactococcus lactis