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A proposed structure for 'family 18' chitinases. A possible function for narbonin
1Biocomputing Research Unit, University of Edinburgh, UK.
FEBS Letters
|October 31, 1994
Summary
Narbonin, a leguminous seed protein, shows similarity to chitinase enzymes. This suggests narbonin may possess chitinase activity or evolved from a functional chitinase.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- Narbonin is a leguminous seed protein.
- Narbonin possesses a TIM barrel structure.
- The function of narbonin is currently unknown.
Purpose of the Study:
- To investigate the potential function of narbonin.
- To determine if narbonin belongs to the chitinase family.
- To explore the evolutionary relationship between narbonin and known chitinases.
Main Methods:
- Sequence similarity analysis comparing narbonin to endo-beta-N-acetylglucosaminidase H.
- Classification of narbonin within the glycosyl hydrolases superfamily, specifically 'Family 18'.
Main Results:
- Narbonin's sequence is significantly similar to Streptomyces plicatus endo-beta-N-acetylglucosaminidase H.
- Narbonin is identified as a member of the 'Family 18' glycosyl hydrolases, a family of chitinases.
- The catalytic domain of 'Family 18' glycosyl hydrolases is proposed to have a TIM barrel structure, consistent with narbonin's structure.
Conclusions:
- It is proposed that narbonin possesses chitinase activity.
- Alternatively, narbonin may have evolved from a functional chitinase through a loss-of-function mechanism.
- Narbonin represents a potential new member of the chitinase enzyme family.