| IED ID | IndEnz0002003487 |
| Enzyme Type ID | protease003487 |
| Protein Name |
D-aminopeptidase EC 3.4.11.19 |
| Gene Name | dap Rsph17029_3981 |
| Organism | Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Rhodobacterales Rhodobacteraceae Cereibacter Cereibacter sphaeroides (Rhodobacter sphaeroides) Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) |
| Enzyme Sequence | MTLDLDALDRALDALPNLFRGPGGVAGVVKDGQVVASRAWGYADLTRRRPMETGTRLPICSISKQFTCGVLLDTLGDTAAYDARVAEFLPQFEGPLPTLRQLCDNQSGLRDYWALTVLQGAEATQTFRREDALPLIARMKTGHFPPGTAYSYCNCNFRIVSEILESETGRALPDLYAERIFGPAGMRTAELTSDTRHPADEVVGYEGSDAVGFFPADNGIFWIGDAGISASLQDMLAYESWIDATRDDENSIYRRISVPPAYVCGTPASYGFGLSHETVAGLKVTGHGGALRGFRAQRFHAADERLSVVVIFNHEASAHAAASSLLAAALGHEAPKGAGPEGWAGQWLDPESGLLLRVGEDAEGLTLRFATGPDRLTVGEDGVPRGAGVSLAREGATLVMNRTSDNLTVRAEPLPVVAVADAGEIAGRYHARELEADLVIEARDGGAYAGFEGLLGAGPMERLHPVGPDVWIVTTRRSMDAPAPGDWTLQVRREGGAVAGLRLGCWLARRIDYARV |
| Enzyme Length | 516 |
| Uniprot Accession Number | A3PRU3 |
| Absorption | |
| Active Site | ACT_SITE 61; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_01960; ACT_SITE 64; /note=Proton donor/acceptor; /evidence=ECO:0000255|HAMAP-Rule:MF_01960 |
| 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:0000255|HAMAP-Rule:MF_01960}. |
| Binding Site | BINDING 480; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_01960 |
| 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:0000255|HAMAP-Rule:MF_01960}; |
| DNA Binding | |
| EC Number | 3.4.11.19 |
| Enzyme Function | FUNCTION: Hydrolyzes N-terminal residues in D-amino acid-containing peptides. {ECO:0000255|HAMAP-Rule:MF_01960}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (1); Chain (1); Region (1) |
| Keywords | Aminopeptidase;Hydrolase;Protease |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 55,262 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |