1B65

Structure of l-aminopeptidase d-ala-esterase/amidase from ochrobactrum anthropi, a prototype for the serine aminopeptidases, reveals a new variant among the ntn hydrolase fold

Summary for 1B65

• Entry DOI: 10.2210/pdb1b65/pdb
• Descriptor: PROTEIN (AMINOPEPTIDASE) (2 entities in total)
• Functional Keywords: hydrolase, peptide degradation, ntn hydrolase
• Biological source: Ochrobactrum anthropi
• Total number of polymer chains: 6
• Total formula weight: 242745.10

Authors

Bompard-Gilles, C.,Villeret, V.,Davies, G.J.,Fanuel, L.,Joris, B.,Frere, J.M.,Van Beeumen, J. (deposition date: 1999-01-20, release date: 1999-07-23, Last modification date: 2023-12-27)

Primary citation

Bompard-Gilles, C.,Villeret, V.,Davies, G.J.,Fanuel, L.,Joris, B.,Frere, J.M.,Van Beeumen, J.
A new variant of the Ntn hydrolase fold revealed by the crystal structure of L-aminopeptidase D-ala-esterase/amidase from Ochrobactrum anthropi.
Structure Fold.Des., 8:153-162, 2000

PubMed Abstract: The L-aminopeptidase D-Ala-esterase/amidase from Ochrobactrum anthropi (DmpA) releases the N-terminal L and/or D-Ala residues from peptide substrates. This is the only known enzyme to liberate N-terminal amino acids with both D and L stereospecificity. The DmpA active form is an alphabeta heterodimer, which results from a putative autocatalytic cleavage of an inactive precursor polypeptide.

PubMed: 10673442
DOI: 10.1016/S0969-2126(00)00091-5

Experimental method

X-RAY DIFFRACTION (1.82 Å)