Cry j I, a major allergen of Japanese cedar pollen, has pectate lyase enzyme activity.
In the course of analyzing the partial amino acid sequences of Cry j I, a major allergen of Japanese cedar (Cryptomeria japonica) pollen, we found a peptide fragment which has a significant homology to some pectate lyase isozymes secreted by plant pathogenic bacteria. Therefore, we investigated whether Cry j I has pectate lyase activity. Cry j I reacted with polygalacturonic acid, resulting in the release of unsaturated uronide products. The optimum temperature and pH for the reaction were 60-70 degrees C and pH 10. The enzymatic reaction had an absolute Ca2+ ion requirement. These characteristics were very compatible with the character of the pectate lyase isozymes reported previously. These results clearly show that Cry j I has pectate lyase activity.
Taniguchi
Y
Y
Fujisaki Institute, Hayashibara Biochemical Laboratories, Inc., Okayama, Japan.
Ono
A
A
Sawatani
M
M
Nanba
M
M
Kohno
K
K
Usui
M
M
Kurimoto
M
M
Matuhasi
T
T
D000485:Allergens / Q000737:chemistry*; D000595:Amino Acid Sequence; D052179:Antigens, Plant; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics; D011058:Pollen / Q000276:immunology*; D011133:Polysaccharide-Lyases / Q000032:analysis*; D017386:Sequence Homology, Amino Acid; D014197:Trees
D000485:Allergens; D052179:Antigens, Plant; C065290:Cry j I protein, Cryptomeria japonica; D010940:Plant Proteins; D011133:Polysaccharide-Lyases; C023911:pectate lyase