Fusarium solani f.pisi

The study of the biosynthesis of D-mannoproteins in other fungi is less developed. It has already been mentioned that the participation of Man-P-Dol as the glycosyl donor in O-glycosylation was demonstrated in Neuro-spora crassa97 and in Fusarium solani f. pisi.56 In the latter, the lipid acceptor was identified as C90- to C110-dolichols. In Hansenula species, O-glycosyla-tion follows the same pathway that is D-mannose linked to L-serine or L-threonine is incorporated by way of Man-P-Dol, and further elongation... 

Purdy, R.E. and Kolattukudy, P.E. 1975. Hydrolysis of plant cutin by plant pathogens purification, amino acids composition, and molecular weight of two isoenzymes of cutinase and a nonspecific esterase from Fusarium solani f. pisi. Biochemistry, 14 2824-31. 

Shaykh, M., Soliday, C.L., and Kolattukudy, P.E. (1977) Proof for the production of cutinase by Fusarium solani f. pisi during penetration into its host. Pi sum sativum. PlantTTiysiol. 60, I70-172. 

Koller, W., Allan, C.R., and Kolattukudy, P.E. (I982) Role of cutinase and cell wall degrading enzymes in infection of Pisum sativum by Fusarium solani f. pisi. Physiol. Plant Pathol. 20. a7-60. 

The PNL exhibits an optimum pH of 9.5 (figure 6) and an optimum temperature of 55" C (figure 7). Lyases catalyze the reaction in an alkaline or in a neutral medium at high temperatures [32] pectin lyase from Phoma medicaginis var. pinodella showed an optimum pH of 7.5 [25], endopectate lyase from Fusarium solani f sp. pisi showed an optimum pH of 9.4 [31], and pectate lyase fi om Rhizoctonia solani showed an optimum pH of 8.0 [34]. 

The enzyme had a requirement for calcium. The addition of EDTA to the reaction mixtures, resulted in complete loss of activity, whereas the addition of CaCl2 increased the activity (figure 8). Presumably, sufficient contaminating calcium ions were present in the dialyzed enzyme and substrate mixture to permit the limited activity of the controls, but apparently these were removed by chelation with EDTA. The optimum concentration was in the range of 5 to 15 M, and higher concentration resulted in a decrease in activity. Phoma medicaginis var. pinodella synthesizes a pectin lyase that lacked an absolute requirement for calcium ions but maximum enzyme activity required the presence of 1 mM Ca [25]. The lyase from Fusarium solani f sp. phaseoli, that is active on pectin and pectic acid, is calcium-dependent [30]. Most of the pectate lyases characterized are calcium-dependent the pectate lyase from Rhizoctonia solani [34] and the endopectate lyase fi om Fusarium solani f sp. pisi [31]. 

Woloshuk CP (1986) Cutinase of Fusarium solani f. sp. pisi mechanism of induction and relatedness to other Fusarium species. PhD thesis, Washington State University, Pullman WA... 

Lin TS, Kolattukudy PE (1978) Induction of a biopolyester hydrolase (cutinase) by low levels of cutin monomers in Fusarium solani f sp. pisi. J Bacteriol 133 942-951... 

Alisch-Mark M, Herrmann A, Zimmermann W (2006) Increase of the hydrophilicity of polyethylene terephthalate fibres by hydrolases from Thermomonospora fusca and Fusarium solani f. sp. pisi. Biotechnol Lett 28 681-685... 

Nimchua, T., Punnapayak, H., and Zimmermann, W. 2007. Comparison of the hydrolysis of polyethylene terephthalate fibers by a hydrolase from Fusarium oxysporum LCH I and Fusarium solani f. sp. pisi. Biotechnology Journal, 2 361. ... 

Figure 3. Comparison of homologous peptides from the two cutinases isolated from Fusarium solani f. sp. pisi and Colletotrichum capsici (W, Ettinger and P.E. Kolattukudy, unpublished results),...

Fernando G, Zimmermann W, Kolattukudy PE (1984) Suberin-grown Fusarium solani f. sp. pisi generates a cutinase like esterase which depolymerizes the aliphatic components of suberin. Plant Pathol 24 143-155... 

Peas, beans Foot rot Fusarium solani f.sp. pisi... 

Flavonoids stimulate spore germination in the soilborne phytopathogenic fungus Fusarium solani. Spore germination of F. solani f. sp. pisi, which causes disease in pea, is stimulated by flavanone hesperetin (141), flavone apigenin (101), the pterocarpan phytoalexin pisatin (142), and so on. In contrast, germination of the bean pathogen F. solani f. sp. phaseoli is stimulated by the pterocarpans maackiain (143) and medicarpin (129), and isoflavones biochanin A (144), and so on but not by pisatin.85... 

Cutinase is induced in the spores of F. solani pisi by cutin, the insoluble polymer (12). This observation, together with the finding that spores of highly virulent isolates of F. solani pisi contain small amounts of cutinase (13), suggested that the actual inducer of cutinase might be the small amounts of cutin monomers generated by the enzyme carried by the spores. In fact, chemically prepared cutin hydrolysate and monomers isolated from it induced cutinase in Fusarium spores (Fig. 5). The most unique monomers of cutin, 10,l6-dihydroxy-Cig acid and 9,10,18-trihydroxy-C]8 acid, that are found nowhere else in nature, were found to be the most potent inducers of cutinase. The enzyme began to appear in the medium... 

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