| IED ID | IndEnz0002014591 |
| Enzyme Type ID | protease014591 |
| Protein Name |
Aminopeptidase YwaD Arginyl aminopeptidase EC 3.4.11.6 BSAP Leucyl aminopeptidase EC 3.4.11.10 |
| Gene Name | ywaD BSU38470 ipa-8r |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MKKLLTVMTMAVLTAGTLLLPAQSVTPAAHAVQISNSERELPFKAKHAYSTISQLSEAIGPRIAGTAAEKKSALLIASSMRKLKLDVKVQRFNIPDRLEGTLSSAGRDILLQAASGSAPTEEQGLTAPLYNAGLGYQKDFTADAKGKIALISRGDLTYYEKAKNAEAAGAKAVIIYNNKESLVPMTPNLSGNKVGIPVVGIKKEDGEALTQQKEATLKLKAFTNQTSQNIIGIKKPKNIKHPDIVYVTAHYDSVPFSPGANDNGSGTSVMLEMARVLKSVPSDKEIRFIAFGAEELGLLGSSHYVDHLSEKELKRSEVNFNLDMVGTSWEKASELYVNTLDGQSNYVWESSRTAAEKIGFDSLSLTQGGSSDHVPFHEAGIDSANFIWGDPETEEVEPWYHTPEDSIEHISKERLQQAGDLVTAAVYEAVKKEKKPKTIKKQMKAKASDIFEDIK |
| Enzyme Length | 455 |
| Uniprot Accession Number | P25152 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys.; EC=3.4.11.6; Evidence={ECO:0000269|PubMed:15668014}; CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.; EC=3.4.11.10; Evidence={ECO:0000269|PubMed:15668014}; |
| DNA Binding | |
| EC Number | 3.4.11.6; 3.4.11.10 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of a range of N-terminal amino acids. {ECO:0000269|PubMed:15668014}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Stable for 20 min at temperatures of up to 80 degrees Celsius. {ECO:0000269|PubMed:15668014}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8-9. {ECO:0000269|PubMed:15668014}; |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (17); Chain (1); Helix (15); Metal binding (6); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Aminopeptidase;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 6HC6; 6HC7; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 49,450 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.6 mM for Arg-pNA {ECO:0000269|PubMed:15668014}; KM=0.85 mM for Lys-pNA {ECO:0000269|PubMed:15668014}; KM=3.6 mM for Leu-pNA {ECO:0000269|PubMed:15668014}; KM=19 mM for Val-pNA {ECO:0000269|PubMed:15668014}; KM=10 mM for Ala-pNA {ECO:0000269|PubMed:15668014}; |
| Metal Binding | METAL 250; /note=Zinc 1; /evidence=ECO:0000250; METAL 262; /note=Zinc 1; /evidence=ECO:0000250; METAL 262; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 295; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 323; /note=Zinc 1; /evidence=ECO:0000250; METAL 401; /note=Zinc 2; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.11.10;3.4.11.6; |