| dc.creator | Canales,Mauricio | |
| dc.creator | Lobos,Sergio | |
| dc.creator | Vicuña,Rafael | |
| dc.date | 1998-08-01 | |
| dc.date.accessioned | 2020-02-17T15:30:09Z | |
| dc.date.available | 2020-02-17T15:30:09Z | |
| dc.identifier | https://scielo.conicyt.cl/scielo.php?script=sci_arttext&pid=S0717-34581998000200006 | |
| dc.identifier.uri | https://revistaschilenas.uchile.cl/handle/2250/128916 | |
| dc.description | Ceriporiopsis subvermispora is a white-rot basidiomycete that produces several isoenzymes of manganese peroxidase (MnP· ). A cDNA of one of them (MnP13-1) has been isolated and sequenced. The deduced aminoacid sequence shows about 60% similarity with the MnPs from Phanerochaete chrysosporium. Based on the crystal structures of MnP and lignin peroxidase (LiP) from P. chrysosporium, and of a peroxidase from Arthromyces ramosus (ARP), we have modeled by homology the three dimensional structure of MnP13-1 using standard modeling procedures. Local molecular mechanics optimization performed in the region corresponding to the binding sites of Ca2+ and Mn2+ in MnP13-1 demonstrated that the stereochemistry and the geometry of binding are conserved in both MnPs. A putative aromatic binding site in MnP13-1 is described. We also report structural differences between the two MnPs, arising from the insertion in MnP13-1 of the sequences TGGN between residues S230 and D231 and TDSP at the C-terminal, both of which may have functional significance. | |
| dc.format | text/html | |
| dc.language | en | |
| dc.publisher | Pontificia Universidad Católica de Valparaíso | |
| dc.rights | info:eu-repo/semantics/openAccess | |
| dc.source | Electronic Journal of Biotechnology v.1 n.2 1998 | |
| dc.title | Molecular modeling of manganese peroxidase from the lignin-degrading fungus Ceriporiopsis subvermispora and structural comparison with other peroxidases | |
