Peptide:N-glycosidase activity found in the early embryos of Oryzias latipes (Medaka fish). The first demonstration of the occurrence of peptide:N-glycosidase in animal cells and its implication for the presence of a de-N-glycosylation system in living organisms.
Peptide:N-glycosidase activity found in the early embryos of Oryzias latipes (Medaka fish). The first demonstration of the occurrence of peptide:N-glycosidase in animal cells and its implication for the presence of a de-N-glycosylation system in living organisms.
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DOI：
10.1016/s0021-9258(18)54540-3
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发表时间：
1991-11
期刊：
影响因子：
--
通讯作者：
A. Seko;K. Kitajima;Y. Inoue;S. Inoue
中科院分区：
文献类型：
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作者：
A. Seko;K. Kitajima;Y. Inoue;S. Inoue
最近发现的游离寡糖是某些鱼卵和早期胚胎中典型的以游离二N-乙酰基壳二糖结构终止的复杂类型的糖链(Ishii，K.，Iwa aki，M.，Inoue，S.，Kenny，P.TM.，Komura，H.和Inoue，Y.(1989)J.Biol)。化学。264,1623-1630；Seko，A.，Kitajima，K.，Iwa aki，M.，Inoue，S.和Inoue，Y.(1989)J.Biol。化学。15922-15929；井上，S.，岩崎，M.，石井，K.，北岛，K.和井上，Y.(1989年)J.化学。264,18520-18526)使我们发现了一种酶，该酶通过水解水稻胚胎中的β-天门冬氨基-葡萄糖胺连接，负责将N-连接的糖链从糖蛋白中分离出来。将N-氨基-4-(N-乙酰-β-氨基葡萄糖基)天冬酰胺酰胺酶或N-糖苷酶(PNGase)进行了部分纯化(2090倍)，并通过对反应产物的分析和鉴定确定了该酶的作用部位。这是第一次证明PNGase存在于动物来源，尽管有报道称PNGase存在于各种植物提取物和细菌中。因此，现在证明了这种类型的酶的共性，并提出了PNGase作为一种基本的生物过程在去N-糖基化中可能的生理作用。
The recent discovery of free oligosaccharides typical for the complex type of glycan chains terminating with a free di-N-acetylchitobiosyl structure in certain fish eggs and early embryos (Ishii, K., Iwasaki, M., Inoue, S., Kenny, P. T. M., Komura, H., and Inoue, Y. (1989) J. Biol. Chem. 264, 1623-1630; Seko, A., Kitajima, K., Iwasaki, M., Inoue, S., and Inoue, Y. (1989) J. Biol. Chem. 264, 15922-15929; Inoue, S., Iwasaki, M., Ishii, K., Kitajima, K., and Inoue, Y. (1989) J. Biol. Chem. 264, 18520-18526) led us to find an enzyme responsible for detachment of N-linked glycan chains from glycoproteins by hydrolyzing the beta-aspartyl-glucosylamine linkage in Oryzias latipes embryos. The enzyme, peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase or peptide:N-glycosidase (PNGase), was partially (2090-fold) purified, and the reaction site at which this enzyme acts was specified by analysis and identification of the reaction products. This is the first demonstration showing PNGase in animal sources, although the presence of PNGases was reported in a variety of plant extracts and bacteria. Thus, the commonality of this type of enzyme is now demonstrated, and the possible physiological role of PNGase in de-N-glycosylation as a basic biologic process is proposed.