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Literature summary for 3.5.1.17 extracted from

  • Koreishi, M.; Kawasaki, R.; Imanaka, H.; Imamura, K.; Takakura, Y.; Nakanishi, K.
    Efficient Nepsilon-lauroyl-L-lysine production by recombinant epsilon-lysine acylase from Streptomyces mobaraensis (2009), J. Biotechnol., 141, 160-165.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, sequence comparisons, overexpression as soluble secreted enzyme in Streptomyces lividans strain TK24, subcloning in Escherichia coli strain DH5alpha Streptomyces mobaraensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55816
-
x * 55816, sequence calculation Streptomyces mobaraensis

Organism

Organism UniProt Comment Textmining
Streptomyces mobaraensis C4B800
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme to homogeneity Streptomyces mobaraensis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2500 2800 purified recombinant enzyme, pH not specified in the publication, temperature not specified in the publication Streptomyces mobaraensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information Sm-ELA catalyzes not only the hydrolysis of various Nepsilon-acyl-L-lysines but also the synthesis of Nepsilon-acyl-L-lysines from L-lysine hydrochloride and medium-/long-chain fatty acids, including Nepsilon-lauroyl-L-lysine Streptomyces mobaraensis ?
-
?
N6-acyl-L-lysine + H2O the enzyme specifically catalyzes hydrolysis of the epsilon-amide bond in various Nepsilon-acyl-L-lysines Streptomyces mobaraensis a carboxylate + L-lysine
-
?

Subunits

Subunits Comment Organism
? x * 55816, sequence calculation Streptomyces mobaraensis

Synonyms

Synonyms Comment Organism
ELA
-
Streptomyces mobaraensis
epsilon-lysine acylase
-
Streptomyces mobaraensis
More the enzyme belongs to the YtcJ-like metal-dependent amidohydrolase family, which is further characterized as the metallo-dependent hydrolase superfamily Streptomyces mobaraensis