AC   MF_01960;
DC   Protein; auto
TR   HAMAP; MF_01960; -; 1; level=0
XX
Names: D_aminopeptidase
XX
ID   DAP
DE   RecName: Full=D-aminopeptidase;
DE            EC=3.4.11.19;
GN   Name=dap;
XX
CC   -!- FUNCTION: Hydrolyzes N-terminal residues in D-amino acid-containing
CC       peptides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal D-amino acid from a peptide, Xaa-|-
CC         Yaa-, in which Xaa is preferably D-Ala, D-Ser or D-Thr. D-amino acid
CC         amides and methyl esters also are hydrolyzed, as is glycine amide.;
CC         EC=3.4.11.19;
CC   -!- ACTIVITY REGULATION: Inhibited by beta-lactam compounds such as 6-
CC       aminopenicillic acid, 7-aminocephalosporanic acid, benzylpenicillin and
CC       ampicillin. Inhibited by p-chloromercuribenzoate.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the peptidase S12 family.
XX
DR   Pfam; PF00144; Beta-lactamase; 1; trigger=no
DR   Pfam; PF07930; DAP_B; 1; trigger=no
DR   Pfam; PF07932; DAP_C; 1; trigger=no
XX
KW   Aminopeptidase
KW   Hydrolase
KW   Protease
XX
GO   GO:0004177; F:aminopeptidase activity
XX
FT   From: DAP_BRUAN (Q9ZBA9)
FT   REGION          477..487
FT                   /note="Important for specificity"
FT   ACT_SITE        62
FT                   /note="Nucleophile"
FT   Condition: S
FT   ACT_SITE        65
FT                   /note="Proton donor/acceptor"
FT   Condition: K
FT   BINDING         481
FT                   /ligand="substrate"
FT   Condition: D
XX
Size: 516-525;
Related: None;
Template: Q9ZBA9;
Scope:
 Bacteria; Alphaproteobacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.14 2022/05/14
//