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Literature summary extracted from

  • Okazaki, S.; Suzuki, A.; Komeda, H.; Yamaguchi, S.; Asano, Y.; Yamane, T.
    Crystal structure and functional characterization of a D-stereospecific amino acid amidase from Ochrobactrum anthropi SV3, a new member of the penicillin-recognizing proteins (2007), J. Mol. Biol., 368, 79-91.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.16.4 into the pET15b vector for expression in Escherichia coli cells Brucella anthropi

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.16.4 the crystal structures of native D-amino acid amidase and of the D-phenylalanine/D-amino acid amidase complex are determined at 2.1 and at 2.4 A resolution, respectively Brucella anthropi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.16.4 D-amino acid amide + H2O Brucella anthropi
-
 D-amino acid + ammonia
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.16.4 Brucella anthropi Q9LCC8 Ochrobactrum anthropi SV3
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.16.4
-
 Brucella anthropi

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.16.4 D-amino acid amide + H2O
-
 Brucella anthropi D-amino acid + ammonia
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.16.4 D-amino acid amidase lacks peptidase activity Brucella anthropi
3.4.16.4 DAA
-
 Brucella anthropi