Covalent structure of soybean seed coat peroxidase.
Peroxidase from soybean seed coat (SBP) is very stable at high temperature, extremes of pH, and in organic solvent. At the same time, it is highly reactive towards both organic and inorganic substrates, similar to horseradish peroxidase. SBP has a wide range of potential applications, and its structure is of particular interest for engineering purposes and as a model for stable heme peroxidases. The covalent structure of SBP has been determined by Edman sequencing and MALDI-TOF MS. SBP is a highly heterogeneous glycoprotein with MS determined masses from 39 to 41 kDa. The mature protein consists of 306 residues starting with pyrrolidone carboxylic acid. Seven glycosylation sites have been observed, although some sites were only partially glycosylated. No putative plant peroxidases were orthologous to SBP. However, SBP showed greater than 70% amino acid sequence identity to peroxidases from other legumes recruited in various defense responses.
Welinder
Karen G
KG
Department of Protein Chemistry, Institute of Molecular Biology, University of Copenhagen, Øster Farimagsgade 2A, DK-1353 Copenhagen K, Denmark. welinder@bio.auc.dk
Larsen
Yvonne B
YB
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D009195:Peroxidase / Q000737:chemistry*; D012639:Seeds / Q000737:chemistry* / Q000201:enzymology / Q000378:metabolism; D013025:Glycine max / Q000737:chemistry* / Q000201:enzymology / Q000378:metabolism
D009195:Peroxidase