IED ID | IndEnz0002018979 |
Enzyme Type ID | protease018979 |
Protein Name |
D-aminopeptidase EC 3.4.11.19 |
Gene Name | dap BSUIS_B0939 |
Organism | Brucella suis (strain ATCC 23445 / NCTC 10510) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Hyphomicrobiales Brucellaceae Brucella/Ochrobactrum group Brucella Brucella suis Brucella suis bv. 2 Brucella suis (strain ATCC 23445 / NCTC 10510) |
Enzyme Sequence | MPNIDLPTLEAFVHAIPQNYKGPGGAVAVVRNGEIVLRHAWGFADLAARKAMTPETRMPICSVSKQFTCAVLLDCIGEPEMLDSALAAYLDQFEDGRPAVRDLCNNQSGLRDYWALTVLCGAAPEGIFLPDQAQNLLRRLKTTHFAPGTHYSYCNGNFRILADLIEQHTGRSLADLLAERIFAPAAMKTAELIPDTALFNECTGYEGDTVRGFLPAINRIHWLGDAGICASLDDMIAWEQFIDRTRHDENGLYRRLSSPQTFADGAPAPYGFGLKFEETGGKRLTGHGGALRGWRCQRWHCADERISTIVMFNFEGNASDAALKMMNAALGIPPAKPVRAQANPGWFGSWLNPETGLVLSLEDAGGGRMKARFGTGPEIMDISGENEAQSSMTTLRRDGDMIHLARKDENLHLAMHRLKGEARQDIAGRYRSDELEADLLLVSEGGAIYGAFEGFLGKSDMYPLYAAGPDVWLLPVQRSMDAPSPGEWKLVFHRDAAGRITGVTVGCWLARGVEYKRL |
Enzyme Length | 518 |
Uniprot Accession Number | A9WVV8 |
Absorption | |
Active Site | ACT_SITE 62; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_01960; ACT_SITE 65; /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 481; /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 | 56,873 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |