Glycans of higher plant peroxidases: recent observations and future speculations.
Plant peroxidases are composed of a peptide and associated heme, calcium and glycans. The 3D structure of the major cationic peanut peroxidase has revealed the sites of the heme and calcium. But the diffraction of the glycans was not sufficient to show their structure. This review presents research that has been executed to obtain putative glycans and their binding sites, and to gain an indirect insight into these glycans. It also offers approaches that will be used to determine the function of the glycans on the peanut peroxidase. Some comparisons are made with other plant glycoproteins including peroxidases from plants other than peanut.
van Huystee
R B
RB
Department of Plant Sciences, The University of Western Ontario London, Canada.
McManus
M T
MT
D010367:Arachis / Q000201:enzymology; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000378:metabolism; D006031:Glycosylation; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010544:Peroxidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011134:Polysaccharides / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
D010940:Plant Proteins; D011134:Polysaccharides; D010544:Peroxidases; D006026:Glycoside Hydrolases