| IED ID | IndEnz0002016287 |
| Enzyme Type ID | protease016287 |
| Protein Name |
Probable dipeptidyl peptidase 3 EC 3.4.14.4 Dipeptidyl aminopeptidase III Dipeptidyl arylamidase III Dipeptidyl peptidase III DPP III |
| Gene Name | YOL057W O1232 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MSHFFADHDAPLSMLSVKTEYFPQLTDKEQKYAHFMSKASHAGSRVVMRQVSHESEPIFDLILAIHSKLNGKYPEDDITQKQQTGLYLEYVSQFLSNLGNFKSFGDTKFIPRCEVKFFKQLLELAKINPCSSPLTLSPVDVNHEFTSHHLFSTINELIDIGIYHVEEKAALLGFPSQGYTSAYYLGLPVTPEDMALLKEQLFAELAILPENTRINKVGENSFQIWVASENVKNQITETYPSGQITLSNAVTKVEFIFGDHSREMRLVASYLKEAQKFAANDTQKAMLQEYINHFVTGSSQAHKEAQKLWVKDISPVIETNIGFIETYREPSGIIGEFESLVAIQNKERTAKFSSLVNNAEEFISLLPWSKDYEKPIFNPPDFTSLEVLTFTGSGIPAGINIPNYDDVRLKIGFKNVSLGNILSAAAKSSSKHPPSFISQEDRPIFEKYQSDSFEVQVGIHELLGHGSGKLLTEFTDGFNFDKENPPLGLDGKPVSTYYKVGETWGSKFGQLAGPFEECRAEVIAMFLLTNKKILDIFGFHDVESQDKVIYAGYLQMARAGLLALEYWNPKTGKWGQPHMQARFSIMKTFMKHSTDKNFLKLEMNSTNDDFAIKLDKSLIKTAGHECVKDYLKHLHVYKCSGDVEQGSKYFIDRSTVTPDLASLRDIVLSKRLPRRQFIQSNSYIDDNNKVTLKEYDETPQGMLQSFLDREL |
| Enzyme Length | 711 |
| Uniprot Accession Number | Q08225 |
| Absorption | |
| Active Site | ACT_SITE 461; /evidence=ECO:0000250|UniProtKB:O55096 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.; EC=3.4.14.4; |
| DNA Binding | |
| EC Number | 3.4.14.4 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (25); Chain (1); Erroneous initiation (1); Helix (35); Metal binding (3); Turn (9) |
| Keywords | 3D-structure;Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3CSK; |
| Mapped Pubmed ID | 18550518; 19825391; 22306662; 23362197; 24136327; 27693354; |
| Motif | |
| Gene Encoded By | |
| Mass | 80,510 |
| Kinetics | |
| Metal Binding | METAL 460; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9NY33; METAL 465; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9NY33; METAL 517; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9NY33 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.14.4; |