CHARACTERIZATION OF THE GENE ENCODING MANGANESE PEROXIDASE ISOZYME-3 FROM PHANEROCHAETE-CHRYSOSPORIUM

Citation
M. Alic et al., CHARACTERIZATION OF THE GENE ENCODING MANGANESE PEROXIDASE ISOZYME-3 FROM PHANEROCHAETE-CHRYSOSPORIUM, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1338(1), 1997, pp. 1-7
Citations number
36
Categorie Soggetti
Biology,Biophysics
ISSN journal
01674838
Volume
1338
Issue
1
Year of publication
1997
Pages
1 - 7
Database
ISI
SICI code
0167-4838(1997)1338:1<1:COTGEM>2.0.ZU;2-7
Abstract
The gene encoding manganese peroxidase isozyme 3 (MnP3) from the white -rot basidiomycete Phanerochaete chrysosporium was cloned and sequence d, The mnp3 gene encodes a mature protein of 357 amino acids with a 25 amino-acid signal peptide. The amino acids involved in peroxidase fun ction, as well as those forming the Mn-II binding site and those invol ved in disulfide bond formation, are conserved in the MnP3 sequence. T he mnp3 gene has six introns, indicating that the sequenced P. chrysos porium mnp genes can be divided into three subfamilies on the basis of intron-exon structure. The mnp3 gene promoter contains putative metal response elements and heat shock elements which may be involved in th e regulation of mnp gene transcription by Mn, the substrate for the en zyme, and by heat shock. (C) 1997 Elsevier Science B.V.