| IED ID | IndEnz0002003938 |
| Enzyme Type ID | protease003938 |
| Protein Name |
D-aminopeptidase EC 3.4.11.19 |
| Gene Name | dap |
| Organism | Brucella anthropi (Ochrobactrum anthropi) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Hyphomicrobiales Brucellaceae Brucella/Ochrobactrum group Brucella Brucella anthropi (Ochrobactrum anthropi) |
| Enzyme Sequence | MSKFDTSALEAFVRHIPQNYKGPGGVVAVVKDGEVVLQHAWGFADLRTRTPMTLDTRMPICSVSKQFTCAVLLDAVGEPELLDDALEAYLDKFEDERPAVRDLCNNQSGLRDYWALSVLCGADPEGVFLPAQAQSLLRRLKTTHFEPGSHYSYCNGNFRILADLIEAHTGRTLVDILSERIFAPAGMKRAELISDTALFDECTGYEGDTVRGFLPATNRIQWMGDAGICASLNDMIAWEQFIDATRDDESGLYRRLSGPQTFKDGVAAPYGFGLNLHETGGKRLTGHGGALRGWRCQRWHCADERLSTIAMFNFEGGASEVAFKLMNIALGVSSSEVSRVEADSAWFGSWLDDETGLVLSLEDAGHGRMKARFGTSPEMMDVVSANEARSAVTTIRRDGETIELVRASENLRLSMKRVKGEAKHDIIGRYHSDELDADLLLVSEGGAIYGAFEGFLGKSDMYPLYSVGSDVWLLPVQRSMDAPSPGEWKLVFRRDDKGEITGLSVGCWLARGVEYRRVQP |
| Enzyme Length | 520 |
| Uniprot Accession Number | Q9ZBA9 |
| Absorption | BIOPHYSICOCHEMICAL PROPERTIES: Absorption: Abs(max)=281 nm {ECO:0000269|PubMed:2760064}; |
| Active Site | ACT_SITE 62; /note=Nucleophile; /evidence=ECO:0000305; ACT_SITE 65; /note=Proton donor/acceptor; /evidence=ECO:0000305 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by beta-lactam compounds such as 6-aminopenicillic acid, 7-aminocephalosporanic acid, benzylpenicillin and ampicillin. Inhibited by p-chloromercuribenzoate. {ECO:0000269|PubMed:1540587}. |
| Binding Site | BINDING 481; /note=Substrate |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal D-amino acid from a peptide, Xaa-|-Yaa-, in which Xaa is preferably D-Ala, D-Ser or D-Thr. D-amino acid amides and methyl esters also are hydrolyzed, as is glycine amide.; EC=3.4.11.19; Evidence={ECO:0000269|PubMed:16131658, ECO:0000269|PubMed:2760064}; |
| DNA Binding | |
| EC Number | 3.4.11.19 |
| Enzyme Function | FUNCTION: Hydrolyzes N-terminal residues in D-amino acid-containing peptides. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:2760064}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:2760064}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (29); Binding site (1); Chain (1); Helix (19); Initiator methionine (1); Mutagenesis (5); Region (1); Turn (6) |
| Keywords | 3D-structure;Aminopeptidase;Direct protein sequencing;Hydrolase;Protease |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1EI5; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 57,392 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.65 mM for D-alanine amide (at 30 degrees Celsius) {ECO:0000269|PubMed:2760064}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |