αマンノシダーゼ
WordNet
- first in order of importance; "the alpha male in the group of chimpanzees"; "the alpha star in a constellation is the brightest or main star"
- the 1st letter of the Greek alphabet
- the beginning of a series or sequence; "the Alpha and Omega, the first and the last, the beginning and the end"--Revelations
- early testing stage of a software or hardware product; "alpha version"
- any high mountain
PrepTutorEJDIC
- アルファ(ギリシア語アルファベットの第1字A,α;英語のA,aに相当) / アルファ星(星座の主星)
- 高山,高峰
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2018/05/03 18:08:01」(JST)
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Cartoon depiction of the protein Streptococcus pyogenes family GH38 α-Mannosidase created using PyMol.
[1][2]
alpha-mannosidase |
alpha-mannosidase 1, tetramer, Saccharomyces cerevisiae
|
Identifiers |
EC number |
3.2.1.24 |
CAS number |
9025-42-7 |
Databases |
IntEnz |
IntEnz view |
BRENDA |
BRENDA entry |
ExPASy |
NiceZyme view |
KEGG |
KEGG entry |
MetaCyc |
metabolic pathway |
PRIAM |
profile |
PDB structures |
RCSB PDB PDBe PDBsum |
Gene Ontology |
AmiGO / QuickGO |
Search |
PMC |
articles |
PubMed |
articles |
NCBI |
proteins |
|
alpha-Mannosidase (EC 3.2.1.24, alpha-D-mannosidase, p-nitrophenyl-alpha-mannosidase, alpha-D-mannopyranosidase, 1,2-alpha-mannosidase, 1,2-alpha-D-mannosidase, exo-alpha-mannosidase) is an enzyme involved in the cleavage of the alpha form of mannose. Its systematic name is alpha-D-mannoside mannohydrolase.[3][4]
Contents
- 1 Isozymes
- 2 Applications
- 3 Pathology
- 4 References
- 5 External links
Isozymes
Humans express the following three alpha-mannosidase isozymes:
mannosidase, alpha, class 2B, member 1 |
Identifiers |
Symbol |
MAN2B1 |
Alt. symbols |
MANB |
Entrez |
4125 |
HUGO |
6826 |
OMIM |
609458 |
RefSeq |
NM_000528 |
UniProt |
O00754 |
Other data |
EC number |
3.2.1.24 |
Locus |
Chr. 19 cen-q13.1 |
|
mannosidase, alpha, class 2B, member 2 |
Identifiers |
Symbol |
MAN2B2 |
Alt. symbols |
KIAA0935 |
Entrez |
23324 |
HUGO |
29623 |
RefSeq |
NM_015274 |
UniProt |
Q9Y2E5 |
Other data |
EC number |
3.2.1.24 |
Locus |
Chr. 4 p16.2 |
|
mannosidase, alpha, class 2C, member 1 |
Identifiers |
Symbol |
MAN2C1 |
Alt. symbols |
MANA1, MANA |
Entrez |
4123 |
HUGO |
6827 |
OMIM |
154580 |
RefSeq |
NM_006715 |
UniProt |
Q9NTJ4 |
Other data |
EC number |
3.2.1.24 |
Locus |
Chr. 15 q11-qter |
|
Applications
It can be utilized in experiments that determine the effects of the presence or absence of mannose on specific molecules, such as recombinant proteins that are used in vaccine development.[5]
Pathology
A deficiency can lead to alpha-mannosidosis.[6]
References
- ^ "PyMol". Schrodinger. Retrieved 2011-09-14.
- ^ Suits, MDL; Yanping Zhu; Edward J. Taylor; Julia Walton; David L. Zechel; Harry J. Gilbert; Gideon J. Davies (3 February 2010). "Structure and Kinetic Investigation of Streptococcus pyogenes Family GH38 α-Mannosidase". PLoS ONE. 5 (2). doi:10.1371/journal.pone.0009006. Retrieved 2011-09-14.
- ^ Li, Y.-T. (1966). "Presence of α-D-mannosidic linkage in glycoproteins. Liberation of D-mannose from various glycoproteins by α-mannosidase isolated from jack bean meal". J. Biol. Chem. 241 (4): 1010–1012. PMID 5905120.
- ^ Winchester, B. (1984). "Role of α-D-mannosidases in the biosynthesis and catabolism of glycoproteins". Biochem. Soc. Trans. 12 (3): 522–524. PMID 6428944.
- ^ Vlahopoulos S, Gritzapis AD, Perez SA, Cacoullos N, Papamichail M, Baxevanis CN (2009). "Mannose addition by yeast Pichia Pastoris on recombinant HER-2 protein inhibits recognition by the monoclonal antibody herceptin". Vaccine. 27 (34): 4704–8. doi:10.1016/j.vaccine.2009.05.063. PMID 19520203.
- ^ Malm D, Nilssen Ø (2008). "Alpha-mannosidosis". Orphanet J Rare Dis. 3: 21. doi:10.1186/1750-1172-3-21. PMC 2515294 . PMID 18651971.
External links
- GeneReviews/NCBI/NIH/UW entry on Alpha-Mannosidosis
- OMIM entries on Alpha-Mannosidosis
- alpha-Mannosidase 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
|
Enzymes
|
Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
|
Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
|
Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
|
Kinetics |
- Enzyme kinetics
- Eadie–Hofstee diagram
- Hanes–Woolf plot
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
|
Types |
- EC1 Oxidoreductases (list)
- EC2 Transferases (list)
- EC3 Hydrolases (list)
- EC4 Lyases (list)
- EC5 Isomerases (list)
- EC6 Ligases (list)
|
UpToDate Contents
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English Journal
- Rescue of sarcoglycan mutations by inhibition of endoplasmic reticulum quality control is associated with minimal structural modifications.
- Soheili T, Gicquel E, Poupiot J, N'guyen L, Le Roy F, Bartoli M, Richard I.SourceGénéthon, CNRS UMR8587, 1, rue de l'Internationale, 91000 Evry, France.
- Human mutation.Hum Mutat.2012 Feb;33(2):429-39. doi: 10.1002/humu.21659. Epub 2011 Dec 22.
- Sarcoglycanopathies (SGP) are a group of autosomal recessive muscle disorders caused by primary mutations in one of the four sarcoglycan genes. The sarcoglycans (α-, β-, γ-, and δ-sarcoglycan) form a tetrameric complex at the muscle membrane that is part of the dystrophin-glycoprotein complex an
- PMID 22095924
- Towards a stable noeuromycin analog with a d-manno configuration: Synthesis and glycosidase inhibition of d-manno-like tri- and tetrahydroxylated azepanes.
- Deschamp J, Mondon M, Nakagawa S, Kato A, Alonzi DS, Butters TD, Zhang Y, Sollogoub M, Blériot Y.SourceUPMC Univ Paris 06, Institut Parisien de Chimie Moléculaire, UMR CNRS 7201, C-181, 4 place Jussieu F-75005 Paris, France.
- Bioorganic & medicinal chemistry.Bioorg Med Chem.2012 Jan 15;20(2):641-9. Epub 2010 Oct 1.
- Noeuromycin is a highly potent albeit unstable glycosidase inhibitor due to its hemiaminal function. While stable d-gluco-like analogs have been reported, no data are available for d-manno-like structures. A series of tri- and tetrahydroxylated seven-membered iminosugars displaying either a d-manno-
- PMID 20971647
- The lipid linked oligosaccharide donor specificities of Trypanosoma brucei oligosaccharyltransferases.
- Izquierdo L, Mehlert A, Ferguson MA.SourceDivision of Biological Chemistry and Drug Discovery, The College of Life Sciences, University of Dundee, Dundee, UK.
- Glycobiology.Glycobiology.2012 Jan 12. [Epub ahead of print]
- We recently presented a model for site-specific protein N-glycosylation in Trypanosoma brucei whereby the TbSTT3A oligosaccharyltransferase first selectively transfers biantennary Man(5)GlcNAc(2) from the lipid linked oligosaccharide donor Man(5)GlcNAc(2)-PP-Dol to N-glycosylation sequons in acidic
- PMID 22241825
Japanese Journal
- Structural Investigation of the Binding of 5-Substituted Swainsonine Analogues to Golgi alpha-Mannosidase II
- Kuntz Douglas A.,Nakayama Shinichi,Shea Kayla,Hori Hitoshi,Uto Yoshihiro,Nagasawa Hideko,Rose David. R.
- CHEMBIOCHEM 11(5), 673-680, 2010-00-00
- NAID 120004738289
- 1H12-2 異常分泌タンパク質発現に対する麹菌(Aspergillus oryzae)の細胞応答(遺伝子工学,核酸工学,一般講演)
- 横田 淳一,城 大介,多田羅 洋太,一島 英治,新谷 尚弘,五味 勝也
- 日本生物工学会大会講演要旨集 平成18年度, 132, 2006-08-03
- NAID 110007322046
- Cloning and expression of mouse cytosolic alpha-mannosidase (Man2c1)
Related Links
- Alpha-mannosidosis is a rare inherited disorder that causes problems in many organs and tissues of the body. Affected individuals may have intellectual disability, distinctive facial features, and skeletal abnormalities.
- Alpha-mannosidase 2 (EC:3.2.1.114) Alternative name(s): Golgi alpha-mannosidase II Short name: AMan II Short name: Man II Mannosidase alpha class 2A member 1 Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase i Name: ...
Related Pictures
★リンクテーブル★
[★]
- 英
- alpha-mannosidase
- 関
- α-マンノシダーゼ
[★]
- 英
- alpha-mannosidase
- 関
- αマンノシダーゼ
[★]
α、アルファ
- 関
- alfa