βマンノシダーゼ
WordNet
- to remain unmolested, undisturbed, or uninterrupted -- used only in infinitive form; "let her be"
- work in a specific place, with a specific subject, or in a specific function; "He is a herpetologist"; "She is our resident philosopher" (同)follow
- have life, be alive; "Our great leader is no more"; "My grandfather lived until the end of war" (同)live
- be identical to; be someone or something; "The president of the company is John Smith"; "This is my house"
- happen, occur, take place; "I lost my wallet; this was during the visit to my parents house"; "There were two hundred people at his funeral"; "There was a lot of noise in the kitchen"
- have the quality of being; (copula, used with an adjective or a predicate noun); "John is rich"; "This is not a good answer"
- occupy a certain position or area; be somewhere; "Where is my umbrella?" "The toolshed is in the back"; "What is behind this behavior?"
- spend or use time; "I may be an hour"
- stake on the outcome of an issue; "I bet $100 on that new horse"; "She played all her money on the dark horse" (同)wager, play
- the act of gambling; "he did it on a bet" (同)wager
- maintain with or as if with a bet; "I bet she will be there!" (同)wager
- second in order of importance; "the candidate, considered a beta male, was perceived to be unable to lead his party to victory"
- the 2nd letter of the Greek alphabet
- preliminary or testing stage of a software or hardware product; "a beta version"; "beta software"
- beets (同)genus Beta
PrepTutorEJDIC
- 《連結語として補語を伴なって…『である』,…だ,…です / 《位置・場所を表す語句を伴って》(…に)『ある』,いる(occupy a place or situation) / 〈物事が〉『存在する』,ある(exist);〈生物が〉生存する,生きている(live) / 行われる,起こる,発生する(take place, occur) / 存続する,そのままでいる(remain as before) / 《『be to』 do》 / …する予定である,…することになっている / …すべきだ / 《受動態の不定詞を伴って》…できる / 《命令》…するのだ / 《条件節に》…する意図がある / 《『if…were to』 do》…するとしたなら / 《『be』 do『ing』》《進行形》 / 《進行中の動作》…している,しつつある / 《近い未来》…しようとしている,するつもり / 《動作の反復》(いつも)…している / 《『be』+『他動詞の過去分詞』》《受動態》…される,されている / 《『be』+『自動詞の過去分詞』》《完了形》…した[状態にある]
- 『かけ』・(…との)かけ《+『with』+『名』》 / かけた物(金) / かけの対象 / 〈金・物〉'を'『かける』 / (かけ事・ゲームなどで)〈人〉‘と'『かけをする』《+『名』〈人〉+『on』+『名』》 / (…に)『かける』《+『on』(『against』)+『名』(one's do『ing』)》
- ベータ(ギリシア語アルファベットの第2文字;B,β;英語のB,b に遭当)
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2018/07/23 07:23:20」(JST)
[Wiki en表示]
For other uses of the term "MANBA", see Manba (disambiguation).
| MANBA |
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| Identifiers |
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| Aliases | MANBA, MANB1, mannosidase beta |
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| External IDs | MGI: 88175 HomoloGene: 4317 GeneCards: MANBA |
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| Gene location (Human) |
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| | Chr. | Chromosome 4 (human)[1] |
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| | Band | 4q24 | Start | 102,630,770 bp[1] |
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| End | 102,760,994 bp[1] |
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| Gene location (Mouse) |
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| | Chr. | Chromosome 3 (mouse)[2] |
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| | Band | 3 G3|3 62.65 cM | Start | 135,485,611 bp[2] |
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| End | 135,571,404 bp[2] |
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| Gene ontology |
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| Molecular function | • hydrolase activity
• hydrolase activity, hydrolyzing O-glycosyl compounds
• mannose binding
• hydrolase activity, acting on glycosyl bonds
• beta-mannosidase activity
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| Cellular component | • lysosome
• lysosomal lumen
• plasma membrane
• azurophil granule membrane
• intracellular membrane-bounded organelle
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| Biological process | • metabolism
• cellular protein modification process
• oligosaccharide catabolic process
• neutrophil degranulation
• carbohydrate metabolic process
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| Sources:Amigo / QuickGO |
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| Orthologs |
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| Species | Human | Mouse |
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| Entrez | | |
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| Ensembl | | |
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| UniProt | | |
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| RefSeq (mRNA) | | |
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| RefSeq (protein) | | |
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| Location (UCSC) | Chr 4: 102.63 – 102.76 Mb | Chr 3: 135.49 – 135.57 Mb |
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| PubMed search | [3] | [4] |
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| Wikidata |
| View/Edit Human | View/Edit Mouse |
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| Beta-mannosidase |
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| Identifiers |
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| EC number |
3.2.1.25 |
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| CAS number |
9025-43-8 |
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| Databases |
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| IntEnz |
IntEnz view |
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| BRENDA |
BRENDA entry |
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| ExPASy |
NiceZyme view |
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| KEGG |
KEGG entry |
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| MetaCyc |
metabolic pathway |
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| PRIAM |
profile |
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| PDB structures |
RCSB PDB PDBe PDBsum |
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| Gene Ontology |
AmiGO / QuickGO |
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| Search |
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| PMC |
articles |
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| PubMed |
articles |
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| NCBI |
proteins |
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Beta-mannosidase (EC 3.2.1.25, mannanase, mannase, beta-D-mannosidase, beta-mannoside mannohydrolase, exo-beta-D-mannanase, lysosomal beta A mannosidase) is an enzyme with systematic name beta-D-mannoside mannohydrolase, which is in humans encoded by the MANBA gene.[5][6][7][8][9][10] This enzyme catalyses the following chemical reaction
- Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides
This gene encodes a member of the glycosyl hydrolase 2 family. The encoded protein localizes to the lysosome where it is the final exoglycosidase in the pathway for N-linked glycoprotein oligosaccharide catabolism. Mutations in this gene are associated with beta-mannosidosis, a lysosomal storage disease that has a wide spectrum of neurological involvement.[5]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000109323 - Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028164 - Ensembl, May 2017
- ^ "Human PubMed Reference:".
- ^ "Mouse PubMed Reference:".
- ^ a b "Entrez Gene: mannosidase".
- ^ Chen H, Leipprandt JR, Traviss CE, Sopher BL, Jones MZ, Cavanagh KT, Friderici KH (February 1995). "Molecular cloning and characterization of bovine beta-mannosidase". J. Biol. Chem. 270 (8): 3841–8. doi:10.1074/jbc.270.8.3841. PMID 7876128.
- ^ Adams, M.; Richtmyer, N.K. & Hudson, C.S. (1943). "Some enzymes present in highly purified invertase preparations; a contribution to the study of fructofuranosidases, galactosidases, glucosidases and mannosidases". J. Am. Chem. Soc. 65 (7): 1369–1380. doi:10.1021/ja01247a029.
- ^ Bartholomew, B.A. & Perry, A.L. (1973). "The properties of synovial fluid β-mannosidase activity". Biochim. Biophys. Acta. 315 (1): 123–127. doi:10.1016/0005-2744(73)90136-8. PMID 4743897.
- ^ Deuel, H.; Lewuenberger, R. & Huber, G. (1950). "Über den enzymatischen Abbau von Carubin, dem Galaktomannan aus Ceratonia siliqua L". Helv. Chim. Acta. 33 (4): 942–946. doi:10.1002/hlca.19500330424.
- ^ Hylin, J.W. & Sawai, K. (1964). "The enzymatic hydrolysis of Leucaena glauca galactomannan. Isolation of crystalline galactomannan depolymerase". J. Biol. Chem. 239: 990–992. PMID 14165949.
External links
- Human MANBA genome location and MANBA gene details page in the UCSC Genome Browser.
Further reading
- Bolmstedt A, Sjölander S, Hansen JE, et al. (1996). "Influence of N-linked glycans in V4-V5 region of human immunodeficiency virus type 1 glycoprotein gp160 on induction of a virus-neutralizing humoral response". J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 12 (3): 213–20. doi:10.1097/00042560-199607000-00001. PMID 8673525.
- Kalsi G, Kuo PH, Aliev F, et al. (2010). "A systematic gene-based screen of chr4q22-q32 identifies association of a novel susceptibility gene, DKK2, with the quantitative trait of alcohol dependence symptom counts". Hum. Mol. Genet. 19 (12): 2497–506. doi:10.1093/hmg/ddq112. PMC 2876884 . PMID 20332099.
- Levade T, Graber D, Flurin V, et al. (1994). "Human beta-mannosidase deficiency associated with peripheral neuropathy". Ann. Neurol. 35 (1): 116–9. doi:10.1002/ana.410350119. PMID 8285582.
- Hu H, Shioda T, Moriya C, et al. (1996). "Infectivities of human and other primate lentiviruses are activated by desialylation of the virion surface". J. Virol. 70 (11): 7462–70. PMC 190813 . PMID 8892864.
- Yeh JC, Seals JR, Murphy CI, et al. (1993). "Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system". Biochemistry. 32 (41): 11087–99. doi:10.1021/bi00092a019. PMID 8218172.
- Sabourdy F, Labauge P, Stensland HM, et al. (2009). "A MANBA mutation resulting in residual beta-mannosidase activity associated with severe leukoencephalopathy: a possible pseudodeficiency variant". BMC Med. Genet. 10: 84. doi:10.1186/1471-2350-10-84. PMC 2745377 . PMID 19728872.
- Hosgood HD, Zhang L, Shen M, et al. (2009). "Association between genetic variants in VEGF, ERCC3 and occupational benzene haematotoxicity". Occup Environ Med. 66 (12): 848–53. doi:10.1136/oem.2008.044024. PMC 2928224 . PMID 19773279.
- Alkhayat AH, Kraemer SA, Leipprandt JR, et al. (1998). "Human beta-mannosidase cDNA characterization and first identification of a mutation associated with human beta-mannosidosis". Hum. Mol. Genet. 7 (1): 75–83. doi:10.1093/hmg/7.1.75. PMID 9384606.
- Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129 . PMID 16344560.
- Papandreou MJ, Fenouillet E (1997). "Effect of various glycosidase treatments on the resistance of the HIV-1 envelope to degradation". FEBS Lett. 406 (1–2): 191–5. doi:10.1016/S0014-5793(97)00273-1. PMID 9109416.
- Gao J, Arbman G, He L, et al. (2008). "MANBA polymorphism was related to increased risk of colorectal cancer in Swedish but not in Chinese populations". Acta Oncol. 47 (3): 372–8. doi:10.1080/02841860701644052. PMID 17899454.
- Robinson WE, Montefiori DC, Mitchell WM (1987). "Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis". AIDS Res. Hum. Retroviruses. 3 (3): 265–82. doi:10.1089/aid.1987.3.265. PMID 2829950.
- Montefiori DC, Robinson WE, Mitchell WM (1988). "Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1". Proc. Natl. Acad. Sci. U.S.A. 85 (23): 9248–52. doi:10.1073/pnas.85.23.9248. PMC 282716 . PMID 3264072.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928 . PMID 15489334.
- Fenouillet E, Jones I, Powell B, et al. (1993). "Functional role of the glycan cluster of the human immunodeficiency virus type 1 transmembrane glycoprotein (gp41) ectodomain". J. Virol. 67 (1): 150–60. PMC 237347 . PMID 8093218.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241 . PMID 12477932.
- Land A, Braakman I (2001). "Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum". Biochimie. 83 (8): 783–90. doi:10.1016/S0300-9084(01)01314-1. PMID 11530211.
- Blough HA, Pauwels R, De Clercq E, et al. (1986). "Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins". Biochem. Biophys. Res. Commun. 141 (1): 33–8. doi:10.1016/S0006-291X(86)80330-8. PMID 3099781.
- Hart ML, Saifuddin M, Spear GT (2003). "Glycosylation inhibitors and neuraminidase enhance human immunodeficiency virus type 1 binding and neutralization by mannose-binding lectin". J. Gen. Virol. 84 (Pt 2): 353–60. doi:10.1099/vir.0.18734-0. PMID 12560567.
Metabolism: carbohydrate metabolism · glycoprotein enzymes |
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| Anabolism |
- Dolichol kinase
- GCS1
- Oligosaccharyltransferase
|
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| Catabolism |
- Neuraminidase
- Beta-galactosidase
- Hexosaminidase
- mannosidase
- alpha-Mannosidase
- beta-mannosidase
- Aspartylglucosaminidase
- Fucosidase
- NAGA
|
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| Transport | |
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| M6P tagging |
- N-acetylglucosamine-1-phosphate transferase
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Hydrolase: sugar hydrolases (EC 3.2) |
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| 3.2.1: Glycoside hydrolases | | Disaccharidase |
- Sucrase/Sucrase-isomaltase/Invertase
- Maltase
- Trehalase
- Lactase
|
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| Glucosidases |
- Cellulase
- Alpha-glucosidase
- Acid
- Neutral AB
- Neutral C
- Beta-glucosidase
- Debranching enzyme
|
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| 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
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3.2.2: Hydrolysing
N-Glycosyl compounds |
- DNA glycosylases: Oxoguanine glycosylase
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Enzymes |
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| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
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| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
- Enzyme activator
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| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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| Kinetics |
- Enzyme kinetics
- Eadie–Hofstee diagram
- Hanes–Woolf plot
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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| Types |
- EC1 Oxidoreductases (list)
- EC2 Transferases (list)
- EC3 Hydrolases (list)
- EC4 Lyases (list)
- EC5 Isomerases (list)
- EC6 Ligases (list)
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UpToDate Contents
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English Journal
- Differential distribution and biochemical characteristics of hydrolases among developmental stages of Schistosoma mansoni may offer new anti-parasite targets.
- Fernández-Delgado M1, Cortez J1, Sulbarán G1, Matos C1, Incani RN2, Ballén DE1, Cesari IM1.
- Parasitology international.Parasitol Int.2017 Feb;66(1):816-820. doi: 10.1016/j.parint.2016.09.015. Epub 2016 Sep 28.
- Schistosoma mansoni enzymes play important roles in host-parasite interactions and are potential targets for immunological and/or pharmacological attack. The aim of this study was to comparatively assess the presence of hydrolytic activities (phosphatases, glycosidases, aminopeptidases) in soluble (
- PMID 27693560
- Study of Ethanol-Induced Golgi Disorganization Reveals the Potential Mechanism of Alcohol-Impaired N-Glycosylation.
- Casey CA1, Bhat G2, Holzapfel MS3, Petrosyan A2.
- Alcoholism, clinical and experimental research.Alcohol Clin Exp Res.2016 Dec;40(12):2573-2590. doi: 10.1111/acer.13247. Epub 2016 Oct 17.
- BACKGROUND: It is known that ethanol (EtOH) and its metabolites have a negative effect on protein glycosylation. The fragmentation of the Golgi apparatus induced by alteration of the structure of largest Golgi matrix protein, giantin, is the major consequence of damaging effects of EtOH-metabolism o
- PMID 27748959
- Myceliophthora thermophila M77 utilizes hydrolytic and oxidative mechanisms to deconstruct biomass.
- Dos Santos HB1,2,3, Bezerra TM4,3, Pradella JG2, Delabona P2, Lima D2, Gomes E5, Hartson SD6, Rogers J6, Couger B3, Prade R7.
- AMB Express.AMB Express.2016 Dec;6(1):103. Epub 2016 Nov 2.
- Biomass is abundant, renewable and useful for biofuel production as well as chemical priming for plastics and composites. Deconstruction of biomass by enzymes is perceived as recalcitrant while an inclusive breakdown mechanism remains to be discovered. Fungi such as Myceliophthora thermophila M77 ap
- PMID 27807811
Japanese Journal
- Absorption of the Indigestible Disaccharide, β-1,4-Mannobiose, from Coconut by the Rat Portal Vein
- Bioscience, biotechnology, and biochemistry 76(3), 575-577, 2012-03-23
- NAID 10030750907
- Pyridylamination as a means of analyzing complex sugar chains
- Ｐｒｏｃｅｅｄｉｎｇｓ ｏｆ ｔｈｅ Ｊａｐａｎ Ａｃａｄｅｍｙ． Ｓｅｒ． Ｂ： Ｐｈｙｓｉｃａｌ ａｎｄ Ｂｉｏｌｏｇｉｃａｌ Ｓｃｉｅｎｃｅｓ 86(4), 378-390, 2010
- NAID 130000258735
- 食品酵母<I>Candida utilis</I>を用いて調製された短鎖ローカストビーンガムの凍結保護活性
Related Pictures
★リンクテーブル★
[★]
- 英
- beta-mannosidase
- 関
- β-マンノシダーゼ
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- 英
- beta-mannosidase
- 関
- βマンノシダーゼ
[★]
β、ベータ
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