マンノシダーゼ
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/03/11 10:17:45」(JST)
[Wiki en表示]
Mannosidase is an enzyme which hydrolyzes mannose.[1]
There are two types:
- alpha-Mannosidase
- beta-Mannosidase
A deficiency is associated with mannosidosis.
References
- ^ Mannosidases at the US National Library of Medicine Medical Subject Headings (MeSH)
Metabolism: carbohydrate metabolism · glycoprotein enzymes
|
|
Anabolism |
- Dolichol kinase
- GCS1
- Oligosaccharyltransferase
|
|
Catabolism |
- Neuraminidase
- Beta-galactosidase
- Hexosaminidase
- mannosidase
- alpha-Mannosidase
- beta-mannosidase
- Aspartylglucosaminidase
- Fucosidase
- NAGA
|
|
Transport |
|
|
M6P tagging |
- N-acetylglucosamine-1-phosphate transferase
|
|
Hydrolase: sugar hydrolases (EC 3.2)
|
|
3.2.1: Glycoside hydrolases |
Disaccharidase |
- Sucrase/Sucrase-isomaltase/Invertase
- Maltase
- Trehalase
- Lactase
|
|
Glucosidases |
- Cellulase
- Alpha-glucosidase
- Acid
- Neutral AB
- Neutral C
- Beta-glucosidase
- Debranching enzyme
|
|
Other |
- Amylase
- Chitinase
- Lysozyme
- Neuraminidase
- NEU1
- NEU2
- NEU3
- NEU4
- Bacterial neuraminidase
- Viral neuraminidase
- Galactosidases
- alpha-Mannosidase
- Glucuronidase
- Hyaluronidase
- Pullulanase
- Glucosylceramidase
- Galactosylceramidase
- Alpha-N-acetylgalactosaminidase
- Alpha-N-acetylglucosaminidase
- Fucosidase
- Hexosaminidase
- Iduronidase
- Maltase-glucoamylase
- Heparanase
|
|
|
3.2.2: Hydrolysing
N-Glycosyl compounds |
- DNA glycosylases: Oxoguanine glycosylase
|
|
Proteins: enzymes
|
|
Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
|
|
Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
|
|
Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
|
|
Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
|
|
UpToDate Contents
全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.
English Journal
- The signaling pathways underlying starvation-induced upregulation of α-mannosidase Ams1 in Saccharomyces cerevisiae.
- Umekawa M1, Ujihara M2, Makishima K2, Yamamoto S2, Takematsu H3, Wakayama M2.
- Biochimica et biophysica acta.Biochim Biophys Acta.2016 Jun;1860(6):1192-201. doi: 10.1016/j.bbagen.2016.02.018. Epub 2016 Mar 4.
- BACKGROUND: Cells have evolved the mechanisms to survive nutritional shortages in the environment. In Saccharomyces cerevisiae, α-mannosidase Ams1 is known to play a role in catabolism of N-linked free oligosaccharides in the cytosol. Although, this enzyme is also known to be transported selectivel
- PMID 26947009
- Terminal alpha-d-mannosides are critical during sea urchin gastrulation.
- Aleksanyan H1, Liang J1, Metzenberg S1, Oppenheimer SB2.
- Zygote (Cambridge, England).Zygote.2016 May 18:1-8. [Epub ahead of print]
- The sea urchin embryo is a United States National Institutes of Health (NIH) designated model system to study mechanisms that may be involved in human health and disease. In order to examine the importance of high-mannose glycans and polysaccharides in gastrulation, Lytechinus pictus embryos were in
- PMID 27189235
- Epimerization of C5 of an N-hydroxypyrrolidine in the synthesis of swainsonine related iminosugars.
- Qian BC1, Kamori A2, Kinami K2, Kato A2, Li YX3, Fleet GW4, Yu CY5.
- Organic & biomolecular chemistry.Org Biomol Chem.2016 May 11;14(19):4488-98. doi: 10.1039/c6ob00531d.
- Epimerization of C5 of an N-hydroxypyrrolidine ring by regioselective oxidation to a nitrone followed by diastereoselective reduction provides a new approach to the synthesis of swainsonine and related compounds. The only protection in the synthesis of the potent mannosidase inhibitor DIM (1,4-dideo
- PMID 27093691
Japanese Journal
- EDEM2 initiates mammalian glycoprotein ERAD by catalyzing the first mannose trimming step.
- Ninagawa Satoshi,Okada Tetsuya,Sumitomo Yoshiki,Kamiya Yukiko,Kato Koichi,Horimoto Satoshi,Ishikawa Tokiro,Takeda Shunichi,Sakuma Tetsushi,Yamamoto Takashi,Mori Kazutoshi
- The Journal of cell biology 206(3), 347-356, 2014-08-04
- … We therefore conducted transcription activator-like effector nuclease-mediated gene knockout analysis in human cell line and found that all endogenous EDEMs possess mannosidase activity. …
- NAID 120005468381
- Trimming of glucosylated N-glycans by human ER α1,2-mannosidase Ⅰ
- Aikawa Jun-ichi,Takeda Yoichi,Matsuo Ichiro [他]
- The journal of biochemistry 155(6), 375-384, 2014-06
- NAID 40020088998
- ER α-1,2-Mannosidase Iは小胞体とゴルジ体のどちらに局在するのか?
- 芳賀 淑美
- Trends in Glycoscience and Glycotechnology 26(150), 103-105, 2014
- NAID 130004679146
Related Links
- 分裂酵母(Schizosaccharomyces pombe)にはER α-mannosidase(ER Man)が存在するにもかかわらず、今まで酵素活性は検出されていなかった。今回彼らは、分裂酵母のER Man破壊株を作製して実験したところ、糖タンパク質のERADが ...
- 特徴 2015年3月より製品付属の反応バッファーの名称および名称が変更されました。詳細はこちら 説明: α1-2,3 Mannosidaseはオリゴ糖からα1-2およびα1-3結合型D-マンノピラノシル残基を高い特異性で切断するエキソグリコシダーゼである。
★リンクテーブル★
[★]
マンノシダーゼ欠損症
- 関
- mannosidosis