Chitinases functions

Fuhrman, J.A., Lee, J. and Dalamagas, D. (1995) Structure and function of a family of chitinase isozymes from Brugian microfilariae. Experimental Parasitology 80, 672-680. 

Malette, B., Paquette, Y., Merlen, Y. and Bleau, G. (1995) Oviductins possess chitinase and mucin-like domains a lead in the search for biological function of these oviduct-specific ZP-associating glycoproteins. Molecular Reproduction and Development 41, 384-397. 

Venegas, A., Goldstein, J.C., Beauregard, K, Oles, A., Abdulhayoglu, N. and Fuhrman, J.A. (1996) Expression of recombinant microfilarial chitinase and analysis of domain function. Molecular and, Biochemical Parasitology 78, 149-159. 

Fig. 1. SAR cDNA families in tobacco. The relationships and functions of the different gene families from tobacco are described. The asterisk below each class denotes that the cDNA has been expressed in transgenic tobacco. The class I chitinase and class I glucanase are not SAR genes as defined in the text.

Legrand, M., Kauffmann, S., Geoffrey, P. Fritig, B. (1987). Biological function of pathogenesis-related proteins four tobacco pathogenesis-related proteins are chitinases. Proceedings of the National Academy of Sciences (USA) 84, 6750-4. 

Kasprzewska, A. 2003. Plant chitinases—regulation and function. Cell Mol Biol Lett 8 809-824. 

The same disposition of three planar hydrophobic aromatic residues is also adopted by CBM 5 and CBM 10, as other CBMs which have Type A function and unique protein folds. An NMR structure of the 60-residue CBM 5 of an Erwinia chrysanthemi endoglucanase revealed a ski-boot structure, with a flat hydrophobic face corresponding to the sole and heel of the ski-boot. This hydrophobic face contained the three planar hydrophobic residues (two tyrosines and a tryptophan).Also using a CBM 5, but as a chitin binding domain, is the chitinase B of Serratia marcescens (the catalytic domain being GH 18). ... 

Proteases released during the infection process may lead to protein inhomogeneities and product degradation [4, 5]. Several baculovims-encoded proteases and chitinases have heen identified which, upon insect larvae infection, induce hque-faction of the infected host ]44, 45]. The cysteine protease v-cath identified in A. ca-lifornica shows functional homologies to mammahan cathepsin L ]46]. Several studies have focused on the neutrahzation of... 

The solubility problems associated with chitin and chitosan may limit their use in physiological and functional foods. The intestines of most animals lack the ability to produce chitinase and chitosanase. These two enzymes have the ability to hydrolyze chitin and chitosan, respectively. Therefore, they will be excreted unchanged in the feces. On the other hand, chitin and chitosan oligomers are considered to have more physiological functions because they are water soluble and their solutions are less viscous, so they are readily absorbed in the human intestine (Jeon et al., 2000). 

C. E. Vorgias A. Perrakis I. Tews, Structure-Function Studies on the Chitinolytic Enzymes of Serratia marcescens Chitinase and Chitobiase. In Enzyme Engineering Xiif, J. S. Dordick A. J. Russell, Eds. New York Academy of Sciences New York, 1996 Vol. 799, pp 190-192. 

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