Glucanase gene diversity in prokaryotic and eukaryotic organisms.
A number of bacteria and eukaryotes produce extracellular enzymes that degrade various types of polysaccharides including the glucans starch, cellulose and hemicellulose (xylan). The similarities in the modes of expression and specificity of enzyme classes, such as amylase, cellulose and xylanase, suggest common genetic origins for particular activities. Our determination of the extent of similarity between these glucanases suggests that such data may be of very limited use in describing the early evolution of these proteins. The great diversity of these proteins does allow identification of their most highly conserved (and presumably functionally important) regions.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D005075:Biological Evolution; D002477:Cells / Q000201:enzymology*; D005057:Eukaryotic Cells / Q000201:enzymology*; D005784:Gene Amplification; D014644:Genetic Variation; D005087:Glucan 1,4-alpha-Glucosidase / Q000235:genetics; D006026:Glycoside Hydrolases / Q000235:genetics* / Q000378:metabolism; D011387:Prokaryotic Cells / Q000201:enzymology*; D043325:Xylan Endo-1,3-beta-Xylosidase; D000516:alpha-Amylases / Q000235:genetics
D006026:Glycoside Hydrolases; D000516:alpha-Amylases; D005087:Glucan 1,4-alpha-Glucosidase; D043325:Xylan Endo-1,3-beta-Xylosidase