Capnocytophaga gingivalis aminopeptidase: a potential virulence factor

Article Abstract:

The aminopeptidase produced by Capnocytophaga gingivalis, an oral pathogenic bacteria, provides for the bacteria's nutrition and virulence. The enzyme has a pI of 6.3, a molecular mass between 61 and 64 kDa, and an optimal pH of 7.5. The enzyme is a metallo-protease or metal-activated protease and its activity requires Mg2+/Ca2+ and free sulphydryl groups. The enzyme hydrolyzes only those substrates which have free N-terminal residues. The activity of the enzyme is highest at low growth rates while the cell-bound state has constant extracellular activity.

Usage, Bacteria, Pathogenic, Pathogenic bacteria, Bacterial proteins

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Capnocytophaga gingivalis: effects of glucose concentration on growth and hydrolytic enzyme production

Article Abstract:

Glucose may play an important role in making full use of the pathogenic value of Capnocytophaga gingivalis. The bacterium responded to the addition of glucose in chemostat culture as it increased its growth rate by twofold and its biomass yield by fivefold. Glucose enhanced the specific activity of aminopeptidase, trypsin-like protease, acid and alkaline phosphatase and alpha-glucosidase, compared with a control culture grown in a tryptone/thiamine medium.

Glucose

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Lysine aminopeptidase of Aspergillus niger

Article Abstract:

Research describes the cloning and characterization of the first aminopeptidase gene of the M1 family of metallo-aminopeptidases of Aspergillus niger. Results indicate that the enzyme uses lysine, instead of leucine, as its substrate and is inhibited by metal chelators and 1,10-phenanthrolin.

Netherlands, Statistical Data Included, Research, Aspergillus, Amino acids, Enzyme regulation, Amino acid structure-activity relationships

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