(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Eukaryota: NE > Opisthokonta: NE > Fungi: NE > Dikarya: NE > Ascomycota: NE > saccharomyceta: NE > Pezizomycotina: NE > leotiomyceta: NE > dothideomyceta: NE > Dothideomycetes: NE > Pleosporomycetidae: NE > Pleosporales: NE > Pleosporineae: NE > Phaeosphaeriaceae: NE > Paraphoma: NE > unclassified Paraphoma: NE > Paraphoma sp. B47-9: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MKYFTISLLAALATASPIAVPEMQISGDIEARQVGSSKNELETGSASNCP KAILIFARGSTETGNLGTLGAPLGDALESRYGASNVWVQGVGGPYDAALG DNALPRGSSAAAIREGVRLLNLANSKCPNSKVVAGGYSQGAALAAAAISD ASTTVRNQIVGTVLFGYTKNQQNRGGIPGYPQDRLRVYCAVGDLVCEGTL IVLAPHLSYGDEARNEAPAFLISKIGN
Paraphoma-related fungal strain B47-9 secreted a biodegradable plastic (BP)-degrading enzyme which amounted to 68 % (w/w) of the total secreted proteins in a culture medium containing emulsified poly(butylene succinate-co-adipate) (PBSA) as sole carbon source. The gene for this enzyme was found to be composed of an open reading frame consisting of 681 nucleotides encoding 227 amino acids and two introns. Southern blot analysis showed that this gene exists as a single copy. The deduced amino acid sequence suggested that this enzyme belongs to the cutinase (E.C.3.1.1.74) family; thus, it was named P araphoma-related fungus cutinase-like enzyme (PCLE). It degraded various types of BP films, such as poly(butylene succinate), PBSA, poly(butylene adipate-co-terephthalate), poly(epsilon-caprolactone), and poly(DL-lactic acid). It has a molecular mass of 19.7 kDa, and an optimum pH and temperature for degradation of emulsified PBSA of 7.2 and 45 degrees C, respectively. Ca(2+) ion at a concentration of about 1.0 mM markedly enhanced the degradation of emulsified PBSA.
Paraphoma sp. B47-9 Cutinase
