| IED ID | IndEnz0002001488 |
| Enzyme Type ID | protease001488 |
| Protein Name |
Dual function macrocyclase-peptidase POPB EC 3.4.21.26 Prolyl oligopeptidase B POP B Toxin-processing prolyl oligopeptidase |
| Gene Name | POPB GALMADRAFT_78538 |
| Organism | Galerina marginata (strain CBS 339.88) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetidae Agaricales Strophariaceae Galerina Galerina marginata Galerina marginata (strain CBS 339.88) |
| Enzyme Sequence | MSSVTWAPGNYPSTRRSDHVDTYQSASKGEVPVPDPYQWLEESTDEVDKWTTAQADLAQSYLDQNADIQKLAEKFRASRNYAKFSAPTLLDDGHWYWFYNRGLQSQSVLYRSKEPALPDFSKGDDNVGDVFFDPNVLAADGSAGMVLCKFSPDGKFFAYAVSHLGGDYSTIYVRSTSSPLSQASVAQGVDGRLSDEVKWFKFSTIIWTKDSKGFLYQRYPARERHEGTRSDRNAMMCYHKVGTTQEEDIIVYQDNEHPEWIYGADTSEDGKYLYLYQFKDTSKKNLLWVAELDEDGVKSGIHWRKVVNEYAADYNIITNHGSLVYIKTNLNAPQYKVITIDLSKDEPEIRDFIPEEKDAKLAQVNCANEEYFVAIYKRNVKDEIYLYSKAGVQLTRLAPDFVGAASIANRQKQTHFFLTLSGFNTPGTIARYDFTAPETQRFSILRTTKVNELDPDDFESTQVWYESKDGTKIPMFIVRHKSTKFDGTAAAIQYGYGGFATSADPFFSPIILTFLQTYGAIFAVPSIRGGGEFGEEWHKGGRRETKVNTFDDFIAAAQFLVKNKYAAPGKVAINGASNGGLLVMGSIVRAPEGTFGAAVPEGGVADLLKFHKFTGGQAWISEYGNPSIPEEFDYIYPLSPVHNVRTDKVMPATLITVNIGDGRVVPMHSFKFIATLQHNVPQNPHPLLIKIDKSWLGHGMGKPTDKNVKDAADKWGFIARALGLELKTVE |
| Enzyme Length | 730 |
| Uniprot Accession Number | H2E7Q8 |
| Absorption | |
| Active Site | ACT_SITE 577; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084, ECO:0000269|PubMed:29051530"; ACT_SITE 661; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084, ECO:0000269|PubMed:29051530"; ACT_SITE 698; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084, ECO:0000269|PubMed:29051530" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.; EC=3.4.21.26; Evidence={ECO:0000269|PubMed:28866879, ECO:0000269|PubMed:29051530}; |
| DNA Binding | |
| EC Number | 3.4.21.26 |
| Enzyme Function | FUNCTION: Dual function macrocyclase-peptidase involved in the biosynthesis of the highly toxic amanitin toxin family of macrocycles (PubMed:22202811, PubMed:28866879, PubMed:29051530). Cleaves peptide bonds on the C-terminal side of prolyl residues (PubMed:29051530). The enzyme first removes 10 residues from the N-terminus of a 35-residue substrate (PubMed:29051530). Conformational trapping of the 25 amino-acid peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (PubMed:29051530). The enzyme rebinds the 25 amino-acid peptide in a different conformation and catalyzes macrocyclization of the N-terminal eight residues (PubMed:28866879, PubMed:29051530). {ECO:0000269|PubMed:22202811, ECO:0000269|PubMed:28866879, ECO:0000269|PubMed:29051530}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (41); Chain (1); Compositional bias (1); Helix (22); Mutagenesis (5); Region (1); Turn (5) |
| Keywords | 3D-structure;Hydrolase;Protease;Reference proteome;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 5N4B; 5N4C; 5N4D; 5N4E; 5N4F; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 81,781 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=23 uM for the full alpha-amanitin 35mer proprotein {ECO:0000269|PubMed:29051530}; KM=51 uM for the 25mer IWGIGCNPWTAEHVDQTLASGNDIC {ECO:0000269|PubMed:29051530}; KM=19 uM for the 25mer LWGIGCNPWTAEHVDQTLASGNDIC {ECO:0000269|PubMed:29051530}; KM=8 uM for the 25mer IFGIGCNPWTAEHVDQTLASGNDIC {ECO:0000269|PubMed:29051530}; KM=28 uM for the 25mer IWGIGSNPWTAEHVDQTLASGNDIC {ECO:0000269|PubMed:29051530}; KM=10 uM for the 25mer IWGIGCNPWTAEHVDQTLASGNDIS {ECO:0000269|PubMed:29051530}; KM=25 uM for the 19mer IWGIGCNPDQTLASGNDIC {ECO:0000269|PubMed:29051530}; KM=380 uM for the 14mer IWGIGCNPWTAEHV {ECO:0000269|PubMed:29051530}; KM=24.4 uM for the 13mer IWGIGCNPWTAEH {ECO:0000269|PubMed:29051530}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |