Literature DB >> 11068683

A common molecular signature unifies the chitosanases belonging to families 46 and 80 of glycoside hydrolases.

H Tremblay1, J Blanchard, R Brzezinski.   

Abstract

The 3D structure-oriented alignment of the primary sequences of fourteen chitosanases, mainly of bacterial origin and belonging to families 46 and 80 of glycoside hydrolases, resulted in the identification of the following pattern common to all these enzymes: E-[DNQ]-x(8,17)-Y-x(7)-D-x-[RD]-[GP]-x-[TS]-x(3)-[AIVFLY]-G- x(5,11)-D. This pattern is proposed as the molecular signature of the chitosanases from families 46 and 80. It includes several amino acids essential for enzyme activity and (or) stability as shown by site-directed mutagenesis studies on the chitosanase from Streptomyces sp. N174. In particular, it includes two carboxylic residues directly involved in catalysis. We suggest that there is a continuum of sequence similarity between all the analyzed chitosanases, and that all these enzymes should probably be classified in one family.

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Year:  2000        PMID: 11068683

Source DB:  PubMed          Journal:  Can J Microbiol        ISSN: 0008-4166            Impact factor:   2.419


  1 in total

1.  A highly conserved arginine residue of the chitosanase from Streptomyces sp. N174 is involved both in catalysis and substrate binding.

Authors:  Marie-Ève Lacombe-Harvey; Mélanie Fortin; Takayuki Ohnuma; Tamo Fukamizo; Thomas Letzel; Ryszard Brzezinski
Journal:  BMC Biochem       Date:  2013-09-16       Impact factor: 4.059

  1 in total

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