Endo-N-acetyl-β-D-glucosaminidase and peptide-N4-(N-acetyl-glucosaminyl) asparagine amidase activities during germination of Raphanus sativus

• Published in: Phytochemistry (Oxford) 1995-06, Vol.39 (3), p.481-487
• Main Authors: BERGER, S, MENUDIER, A, JULIEN, R, KARAMANOS, Y
• Format: Article
• Language: English
• Subjects: Amidohydrolases - isolation & purification; Amidohydrolases - metabolism; Biological and medical sciences; Biotechnology; Brassica - enzymology; Brassica - physiology; Carbohydrate Sequence; Chromatography, Affinity; Fundamental and applied biological sciences. Psychology; Germination; Germination and dormancy; Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - isolation & purification; Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism; Molecular Sequence Data; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; Plant physiology and development
• ISSN: 0031-9422; 1873-3700
• DOI: 10.1016/0031-9422(95)00001-N

Endo-N-acetyl-beta-D-glucosaminidase (ENGase, EC 3.2.1.96) and peptide-N4-(N-acetyl-beta-D-glucosaminyl) asparagine amidase (PNGase, EC 3.5.1.52) activities were monitored during germination and postgerminative development in Raphanus sativus. The PNGase activity was found in dry seeds and its level was constant during germination and postgermination. The ENGase activity was first detected about 18 hr after the start of imbibition (HAI) and displayed a maximum level at 36 HAI. After 36 HAI the production of both enzymes was constant until days 4-5. Both enzymes displayed substrate specificities corresponding to the potential glycoprotein substrates found in plants. They are in agreement (i) with the hypothesis that ENGase and PNGase are at the origin of the production of 'unconjugated N-glycans' and (ii) with the possibility that protein activity could be regulated by the removal of N-glycans.