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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Cloning and structural analysis of bglM gene coding for the fungal cell wall-lytic beta-1,3-glucan-hydrolase BglM of Bacillus circulans IAM1165.

Bacillus circulans IAM1165 produces isoforms of beta-1,3-glucan-hydrolases. Of these enzymes, the 42-kDa enzyme BgIM degrades Aspergillus oryzae cell walls the most actively. A gene coding for a BgIM precursor consisting of 411 amino acid residues was cloned. The 27 N-terminal amino acid sequence of the precursor is a signal peptide. The 141 C-terminal amino acid sequence showed a motif of carbohydrate-binding module family 13. This domain bound to pachyman, lichenan, and A. oryzae cell walls. The central domain showed a bacterial beta-1,3-glucan-hydrolase motif belonging to glycosyl hydrolase family 16. By removal of the C-terminal domain in the IAM1165 culture, mature BglM was processed to several 27-kDa fragments that hydrolyze a soluble beta-1,3-glucan.[1]

References

  1. Cloning and structural analysis of bglM gene coding for the fungal cell wall-lytic beta-1,3-glucan-hydrolase BglM of Bacillus circulans IAM1165. Asano, T., Taki, J., Yamamoto, M., Aono, R. Biosci. Biotechnol. Biochem. (2002) [Pubmed]
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