| IED ID | IndEnz0002002767 |
| Enzyme Type ID | protease002767 |
| Protein Name |
Aminopeptidase 2, mitochondrial AP-II Aminopeptidase II EC 3.4.11.- YscII |
| Gene Name | APE2 LAP1 YKL157W YKL158W YKL611 YKL612 |
| 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 | MPIVRWLLLKSAVRGSSLIGKAHPCLRSIAAHPRYLSNVYSPPAGVSRSLRINVMWKQSKLTPPRFVKIMNRRPLFTETSHACAKCQKTSQLLNKTPNREILPDNVVPLHYDLTVEPDFKTFKFEGSVKIELKINNPAIDTVTLNTVDTDIHSAKIGDVTSSEIISEEEQQVTTFAFPKGTMSSFKGNAFLDIKFTGILNDNMAGFYRAKYEDKLTGETKYMATTQMEPTDARRAFPCFDEPNLKASFAITLVSDPSLTHLSNMDVKNEYVKDGKKVTLFNTTPKMSTYLVAFIVAELKYVESKNFRIPVRVYATPGNEKHGQFAADLTAKTLAFFEKTFGIQYPLPKMDNVAVHEFSAGAMENWGLVTYRVVDLLLDKDNSTLDRIQRVAEVVQHELAHQWFGNLVTMDWWEGLWLNEGFATWMSWYSCNEFQPEWKVWEQYVTDTLQHALSLDSLRSSHPIEVPVKKADEINQIFDAISYSKGASLLRMISKWLGEETFIKGVSQYLNKFKYGNAKTEDLWDALADASGKDVRSVMNIWTKKVGFPVISVSEDGNGKITFRQNRYLSTADVKPDEDKTIYPVFLALKTKNGVDSSVVLSERSKTIELEDPTFFKVNSEQSGIYITSYTDERWAKLGQQADLLSVEDRVGLVADVKTLSASGYTSTTNFLNLVSKWNNEKSFVVWDQIINSISSMKSTWLFEPKETQDALDNFTKQLISGMTHHLGWEFKSSDSFSTQRLKVTMFGAACAARDADVEKAALKMFTDYCSGNKEAIPALIKPIVFNTVARVGGAENYEKVYKIYLDPISNDEKLAALRSLGRFKEPKLLERTLGYLFDGTVLNQDIYIPMQGMRAHQEGVEALWNWVKKNWDELVKRLPPGLSMLGSVVTLGTSGFTSMQKIDEIKKFFATKSTKGFDQSLAQSLDTITSKAQWVNRDRDVVNKYLKENGYY |
| Enzyme Length | 952 |
| Uniprot Accession Number | P32454 |
| Absorption | |
| Active Site | ACT_SITE 397; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | BINDING 228; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.11.- |
| Enzyme Function | FUNCTION: Involved in the cellular supply of leucine from externally offered leucine-containing dipeptide substrates. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Erroneous gene model prediction (6); Frameshift (2); Glycosylation (2); Metal binding (3); Region (1); Sequence conflict (4); Site (1); Transit peptide (1) |
| Keywords | Aminopeptidase;Cytoplasm;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Mitochondrion;Periplasm;Protease;Reference proteome;Transit peptide;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Periplasm. Cytoplasm. Mitochondrion. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10554772; 11283351; 11805837; 14690591; 16429126; 16554755; 18637841; 18719252; 19185714; 19536198; 20361019; 3286257; 6352682; |
| Motif | |
| Gene Encoded By | |
| Mass | 107,755 |
| Kinetics | |
| Metal Binding | METAL 396; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 400; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 419; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |