| 翻訳と辞書 |
NGLY1
PNGase also known as N-glycanase 1 (EC 3.5.1.52) or peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase is an enzyme that in humans is encoded by the NGLY1 gene. PNGase is a de-''N''-glycosylating enzyme that removes ''N-''linked or asparagine-linked glycans (''N-''glycans) from glycoproteins. More specifically, NGLY1 catalyzes the hydrolysis of the amide bond between the innermost ''N-''acetylglucosamine (GlcNAc) and an Asn residue on an ''N''-glycoprotein, generating a de-''N''-glycosylated protein, in which the ''N-''glycoylated Asn residue is converted to asp, and a 1-amino-GlcNAc-containing free oligosaccharide. Ammonia is then spontaneously released from the 1-amino GlcNAc at physiological pH (<8), giving rise to a free oligosaccharide with an ''N,N’-''diacetylchitobiose structure at the reducing end.
== Discovery ==
Occurrence of cytoplasmic PNGase activity in mammalian cells was first reported in cultured cells. This enzyme differ from other “reagent” PNGases from almond (glycoamidase/PNGase A), or bacteria (''N''-glycanase/PNGase F), that is often used for structural/functional studies of ''N''-glycans, in several enzymatic properties, including the requirement of a reducing reagent for activity and a neutral pH for optimal activity.〔
The gene encoding the cytoplasmic PNGase was first identified in budding yeast, ''Saccharomyces cerevisiae'' and gene orthologues have since been found in wide variety of eukaryotes including mammals. In terms of the tissue distribution of the mouse ''Ngly1'' gene, enzyme activities as well as transcripts were detected in all tissues/organs examined.〔
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
■ウィキペディアで「NGLY1」の詳細全文を読む
スポンサード リンク
| 翻訳と辞書 : 翻訳のためのインターネットリソース |
Copyright(C) kotoba.ne.jp 1997-2016. All Rights Reserved.
|
|