| IED ID | IndEnz0002016385 |
| Enzyme Type ID | protease016385 |
| Protein Name |
Aminopeptidase 2 EC 3.4.11.- |
| Gene Name | APE2 CAALFM_C104400CA CaO19.12664 CaO19.5197 |
| Organism | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Candida Candida albicans (Yeast) Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Enzyme Sequence | MASNNTSQRSGFSSFFCRLKTYFCNHFLCLFVLSFFPLSFRRLCLLCHLCEKSNLWLSSDNSASVVKQEREVLPTNVKPLHYDLTIEPIFDNFTFKGEETIDFQVNEKTNFITLNSLEIEVQEAKIDGKSVTDISFDAGKQTVTFKFDDDLSTGSIAKLYIKFTGELNDKMAGFYRASYQEDGKTKYMATTQMEPTDCRRAFPSYDEPAAKSKFTISLIADKELVCLSNSSEKETVSLDGNKKKVTFQTTPLMSTYLVAFIVGDLRYISNDNYRVPIRVYSTPGTEHLGEYSANIAAQTLKFFDQQFGIDYPYDKLDMVAVPSFSAGAMENCGLVTFRTVDLLIDADNANVNTKQRVTEVVMHELAHQWFGDLVTMEFWDGLWLNEGFATWMSWYACNSLYPDWKVWESYVSDSLQHALTLDALRASHPIEVPVKRADEINQIFDAISYSKGSSLLRMISKWLGEDVFVKGVSNYLKKHKWGNTKTSDLWEALSEASGEDVVKVMDIWTKNIGFPIVKVEEIGNGEIKVTQNRFLATGDVKESEDKTLYPVFLGLKTSEGVDESSVLETRSKTIKLPTSDDFFKINGDQSGIYRTAYEPARWTKLGKAGVEGKLSVEDRVGLVADAGSLASSGFIKTSSLLDLVKSWSKESNYVVWNEILTRIGSIKAALMFEDEATKKALEIFTRDLISEKLKETGWEFSADDSFADQQLKSSLFASAANAEDPEAVAFAKEAFAKFIAGDKKAIHPNLRASIFNTNAKYGDEKTFDELYNIYRNPSSVEEKIAALRSFGRFTKPEILDKVTGLLLQTDIVKQQDIYIPMQGLRAHKLGVEKLWTWLSENWDQIYILLPPGLSMLGSVVTLGTSGFTKEEQKKKVEEFFAQKDNKGYDQSLAQSLDIITAKSKWTDRDAKSIYEWLEANEYTK |
| Enzyme Length | 924 |
| Uniprot Accession Number | Q59KZ1 |
| Absorption | |
| Active Site | ACT_SITE 364; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Inactivated by metal-chelating agents phenanthroline and EDTA. Inhibited by bestatin, an aminopeptidase inhibitor. Not inhibited by pepstatin A and PMSF, inhibitors of aspartic and the serine proteases, respectively. Not inhibited by carboxypeptidase inhibitor. |
| Binding Site | BINDING 194; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.11.- |
| Enzyme Function | FUNCTION: Metalloprotease that specifically hydrolyzes peptides with N-terminal alanine, arginine and leucine residues. {ECO:0000269|PubMed:18637841}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:18637841}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2. {ECO:0000269|PubMed:18637841}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1); Glycosylation (2); Metal binding (3); Modified residue (1); Propeptide (1); Region (1); Sequence conflict (1); Signal peptide (1); Site (1) |
| Keywords | Acetylation;Aminopeptidase;Cell wall;Direct protein sequencing;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:18637841}. |
| Modified Residue | MOD_RES 58; /note=N-acetylserine; partial; /evidence=ECO:0000269|PubMed:18637841 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..45; /evidence=ECO:0000303|PubMed:18637841 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 104,382 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=457 uM for L-alanine-AMC {ECO:0000269|PubMed:18637841}; KM=46.9 uM for L-arginine-AMC {ECO:0000269|PubMed:18637841}; KM=82 uM for L-leucine-AMC {ECO:0000269|PubMed:18637841}; Vmax=16.9 umol/min/mg enzyme for L-alanine-AMC {ECO:0000269|PubMed:18637841}; Vmax=25.4 umol/min/mg enzyme for L-arginine-AMC {ECO:0000269|PubMed:18637841}; Vmax=18.4 umol/min/mg enzyme for L-leucine-AMC {ECO:0000269|PubMed:18637841}; |
| Metal Binding | METAL 363; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 367; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 386; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |