| IED ID | IndEnz0002010819 |
| Enzyme Type ID | protease010819 |
| Protein Name |
A-factor-processing enzyme EC 3.4.24.- Insulin-degrading enzyme homolog |
| Gene Name | STE23 YLR389C L8084.12 |
| 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 | MGVSLLASSSAFVTKPLLTQLVHLSPISLNFTVRRFKPFTCLSRYYTTNPYNMTSNFKTFNLDFLKPDLDERSYRFIELPNKLKALLIQDPKADKAAASLDVNIGAFEDPKNLPGLAHFCEHLLFMGSEKFPDENEYSSYLSKHGGSSNAYTASQNTNYFFEVNHQHLFGALDRFSGFFSCPLFNKDSTDKEINAVNSENKKNLQNDIWRIYQLDKSLTNTKHPYHKFSTGNIETLGTLPKENGLNVRDELLKFHKNFYSANLMKLCILGREDLDTLSDWTYDLFKDVANNGREVPLYAEPIMQPEHLQKIIQVRPVKDLKKLEISFTVPDMEEHWESKPPRILSHLIGHEGSGSLLAHLKKLGWANELSAGGHTVSKGNAFFAVDIDLTDNGLTHYRDVIVLIFQYIEMLKNSLPQKWIFNELQDISNATFKFKQAGSPSSTVSSLAKCLEKDYIPVSRILAMGLLTKYEPDLLTQYTDALVPENSRVTLISRSLETDSAEKWYGTAYKVVDYPADLIKNMKSPGLNPALTLPRPNEFVSTNFKVDKIDGIKPLDEPVLLLSDDVSKLWYKKDDRFWQPRGYIYLSFKLPHTHASIINSMLSTLYTQLANDALKDVQYDAACADLRISFNKTNQGLAITASGFNEKLIILLTRFLQGVNSFEPKKDRFEILKDKTIRHLKNLLYEVPYSQMSNYYNAIINERSWSTAEKLQVFEKLTFEQLINFIPTIYEGVYFETLIHGNIKHEEALEVDSLIKSLIPNNIHNLQVSNNRLRSYLLPKGKTFRYETALKDSQNVNSCIQHVTQLDVYSEDLSALSGLFAQLIHEPCFDTLRTKEQLGYVVFSSSLNNHGTANIRILIQSEHTTPYLEWRINNFYETFGQVLRDMPEEDFEKHKEALCNSLLQKFKNMAEESARYTAAIYLGDYNFTHRQKKAKLVANITKQQMIDFYENYIMSENASKLILHLKSQVENKELNENELDTAKYPTGQLIEDVGAFKSTLFVAPVRQPMKDFEISAPPKLNNSSESE |
| Enzyme Length | 1027 |
| Uniprot Accession Number | Q06010 |
| Absorption | |
| Active Site | ACT_SITE 121; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by chelating agents like EDTA, TPEN and 1,1-phenanthroline, as well as NEM, free cysteine and DTT. {ECO:0000269|PubMed:19750477}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Involved in the N-terminal endoproteolytic cleavage of the P2 precursor of the a-factor mating pheromone. Capable of proteolysing the established mammalian insulin-degrading enzymes (IDEs) substrates amyloid-beta peptide and insulin B-chain. {ECO:0000269|PubMed:15944156, ECO:0000269|PubMed:19750477, ECO:0000269|PubMed:7569998}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:19750477}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.1. {ECO:0000269|PubMed:19750477}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (3) |
| Keywords | Hydrolase;Membrane;Metal-binding;Metalloprotease;Pheromone response;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | INDUCTION: Expressed in both haploid and diploid yeast cells. {ECO:0000269|PubMed:19750477}. |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15944156}; Peripheral membrane protein {ECO:0000269|PubMed:15944156}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10688190; 11805837; 16429126; 16722821; 18719252; 21179020; 22933563; 25620600; 27693354; 28228553; 9725832; |
| Motif | |
| Gene Encoded By | |
| Mass | 117,579 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=215 uM for a synthetic a-factor analog {ECO:0000269|PubMed:19750477}; Vmax=0.49 umol/min/mg enzyme towards a synthetic a-factor analog {ECO:0000269|PubMed:19750477}; |
| Metal Binding | METAL 118; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096; METAL 122; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096; METAL 199; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096 |
| Rhea ID | |
| Cross Reference Brenda |