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Molecular modeling of manganese peroxidase from the lignin-degrading fungus Ceriporiopsis subvermispora and structural comparison with other peroxidases Electron. J. Biotechnol.
Canales,Mauricio; Lobos,Sergio; Vicuña,Rafael.
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...
Tipo: Journal article
Ano: 1998 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34581998000200006
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Molecular dynamics simulations of active site mutants of rat liver arginase Electron. J. Biotechnol.
Canales,Mauricio; Westermeyer,Linda; Carvajal,Nelson.
By using molecular dynamics (MD) simulations and crystallographic data for rat liver arginase, the substrate positions in the active sites of native and mutant forms of the enzyme, were compared and correlated with known kinetic consequences of mutations. The mutants compared were His 141<IMG SRC="/content/vol4/issue3/full/6/flecha2.gif" WIDTH=12 HEIGHT=9>Phe and His 141<IMG SRC="/content/vol4/issue3/full/6/flecha2.gif" WIDTH=12 HEIGHT=9>Asn. The simulations show that mutation His141<IMG SRC="/content/vol4/issue3/full/6/flecha2.gif" WIDTH=12 HEIGHT=9>Asn gives the greatest divergence from the atomic coordinates, when compared with the control native enzyme. The mutant Asp128<IMG SRC="/content/vol4/issue3/full/6/flecha2.gif" WIDTH=12...
Tipo: Journal article
Ano: 2001 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582001000300010
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