A novel 1,3-beta-glucan synthase from the oomycete Saprolegnia monoica

Article Abstract:

A research on the 1,3-beta-glucan synthase from the Saprolegnia monoica was conducted to detect and characterize the organism's activity based on requirements for cofactor or activator. Subjecting the Saprolegnia monoica under strain and related enzymic analysis and techniques were the methodology used. Results showed that S. monoica has two 1,3-beta-glucan synthase activities which include the activity of the enzyme at alkaline pH stimulated by Calcium, Manganese and Magnesium. Furthermore, the 1,3-beta-glucan synthases were also inhibited by guanine-nucleotide binding proteins.

Analysis, Bacteria, G proteins, Microbiological research, Hydrogen-ion concentration

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CHS2, a chitin synthase gene from the oomycete Saprolegnia monoica

Article Abstract:

A PCR experiment was conducted to characterize the chitin-synthase-encoding genes from Saprolegnia monoica. Results show that two chitin synthase (CHS) genes were present in S. monoica which were located in two chromosomes. Furthermore, these CHS genes were also found to be present in two other oomycetes namely, Achlya ambisexualis and Phytophthora capsici. It was concluded that oomycetes and chitinous fungi evolved with conserved chitin synthase system despite their divergent evolution.

Bacterial cell walls

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The properties and localization of Saprolegnia monoica chitin synthase from those other fungi

Article Abstract:

The chitin synthase of Saprolegnia monoica was characterized. Its properties and localization was found different from that of a typical fungi. The enzyme from S. monoica was found having a lower sedimentation coefficient, was not stimulated by phospholipids and was not inhibited by high concentrations of digitonin. However, like other fungi, the enzyme was solubilized by digitonin which remains zymogenic after dissociation.

Fungi

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