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Literature summary for 3.5.1.82 extracted from

  • Yoshimune, K.; Ninomiya, Y.; Wakayama, M.; Moriguchi, M.
    Molecular chaperones facilitate the soluble expression of N-acyl-D-amino acid amidohydrolases in Escherichia coli (2004), J. Ind. Microbiol. Biotechnol., 31, 421-426.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of active D-AGase in Escherichia coli strain JM109 or strain BL21 partially in inclusion bodies, co-expression of chaperones GroELS, DnaKJE, and trigger factor TF Achromobacter xylosoxidans

Organism

Organism UniProt Comment Textmining
Achromobacter xylosoxidans
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
38.1
-
soluble recombinant enzyme from expression without chaperones and trigger factor Achromobacter xylosoxidans
95.8
-
soluble recombinant enzyme from co-expression with chaperones and trigger factor Achromobacter xylosoxidans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is specific for N-acyl-D-glutamate Achromobacter xylosoxidans ?
-
?
additional information the enzyme is specific for N-acyl-D-glutamate Achromobacter xylosoxidans A-6 ?
-
?

Synonyms

Synonyms Comment Organism
D-AGase
-
Achromobacter xylosoxidans
N-acyl-D-glutamate amidohydrolase
-
Achromobacter xylosoxidans