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Aspergillus niger van Tieghem mannosylation: polyprenylphosphate mannosyltransferase specificity
Journal of Lipid Research
|September 1, 1982
Summary
An enzyme in Aspergillus niger transfers mannose from GDP-mannose to polyprenylphosphate. This enzyme shows strict specificity for both the sugar donor and various polyprenylphosphate acceptors.
Area of Science:
- Biochemistry
- Enzymology
- Microbiology
Background:
- Microsomes from Aspergillus niger possess enzymatic activity.
- Polyprenylphosphate is involved in glycosylation pathways.
Purpose of the Study:
- To characterize the enzyme responsible for mannose transfer in Aspergillus niger.
- To investigate the substrate specificity of the mannose transfer enzyme.
Main Methods:
- Enzyme assays using GDP-mannose as the sugar donor.
- Testing various lengths of polyprenylphosphates (C15-C120) as acceptors.
- Utilizing liposome fusion techniques to present acceptors to the enzyme.
Main Results:
- The enzyme efficiently transfers mannose from GDP-mannose.
- All tested polyprenylphosphates (C15-C120) served as acceptors, with the exception of retinylphosphate.
- The enzyme exhibited strict specificity for both the nucleoside diphosphate sugar and the polyprenylphosphate base.
Conclusions:
- Aspergillus niger possesses a specific mannose transfer enzyme.
- This enzyme plays a role in the synthesis of polyprenylmannose derivatives.
- Understanding this enzyme's specificity is crucial for studying glycosylation in fungi.