Weak sequence homologies among chitinases detected by clustering analysis.
The amino acid sequences of various endo-N-acetyl-glucosaminidases (chitinases) have been subjected to hydrophobic cluster analysis. A domain of approximately 145 residues was found to be weakly conserved in chitinase A and B from the bacterium Serriata marcescens, in a chitinase from cucumber (Cucumis sativis) and in the endo-N-acetyl-glucosaminidase H of Streptomyces plicatus. A prediction of the putative active site region was made upon analysis of invariant acidic amino acids. On the basis of primary structure homologies, a classification into families of structurally related proteins is proposed for the enzymes hydrolyzing beta-1,4-N-acetyl-glucosamine linkages.
Henrissat
B
B
Centre de Recherches sur les Macromolécules Végétales, Grenoble, France.
D000117:Acetylglucosamine / Q000378:metabolism; D000595:Amino Acid Sequence; D002688:Chitinases / Q000737:chemistry / Q000235:genetics*; D016000:Cluster Analysis; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010944:Plants / Q000201:enzymology; D012680:Sensitivity and Specificity; D012689:Sequence Homology, Nucleic Acid; D012706:Serratia marcescens / Q000201:enzymology; D012995:Solubility
D002688:Chitinases; D000117:Acetylglucosamine