Berger S, Menudier A, Julien R, Karamanos Y
Institut de Biotechnologie, Université de Limoges, France.
Phytochemistry. 1995 Jun;39(3):481-7. 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.
在萝卜种子萌发和萌发后发育过程中,监测了内切N-乙酰-β-D-葡糖胺酶(ENGase,EC 3.2.1.96)和肽-N4-(N-乙酰-β-D-葡糖胺基)天冬酰胺酶(PNGase,EC 3.5.1.52)的活性。在干燥种子中发现了PNGase活性,其水平在萌发和萌发后保持恒定。ENGase活性在吸胀开始(HAI)约18小时后首次检测到,并在36 HAI时达到最高水平。36 HAI后,两种酶的产生在第4-5天之前保持恒定。两种酶都表现出与植物中发现的潜在糖蛋白底物相对应的底物特异性。它们与以下观点一致:(i)ENGase和PNGase是“未结合的N-聚糖”产生的起源;(ii)蛋白质活性可能通过去除N-聚糖来调节。