マンナナーゼ、マンナン加水分解酵素
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/02/05 10:22:17」(JST)
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For other uses of the term "MANBA", see Manba (disambiguation).
Mannosidase, beta A, lysosomal |
Identifiers |
Symbols |
MANBA ; MANB1 |
External IDs |
OMIM: 609489 MGI: 88175 HomoloGene: 4317 ChEMBL: 3903 GeneCards: MANBA Gene |
EC number |
3.2.1.25 |
Gene ontology |
Molecular function |
• beta-mannosidase activity
• mannose binding
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Cellular component |
• lysosome
• intracellular membrane-bounded organelle
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Biological process |
• carbohydrate metabolic process
• cellular protein modification process
• mannan catabolic process
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Sources: Amigo / QuickGO |
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Orthologs |
Species |
Human |
Mouse |
Entrez |
4126 |
110173 |
Ensembl |
ENSG00000109323 |
ENSMUSG00000028164 |
UniProt |
O00462 |
Q8K2I4 |
RefSeq (mRNA) |
NM_005908 |
NM_027288 |
RefSeq (protein) |
NP_005899 |
NP_081564 |
Location (UCSC) |
Chr 4:
102.63 – 102.76 Mb |
Chr 3:
135.49 – 135.57 Mb |
PubMed search |
[1] |
[2] |
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Beta-mannosidase |
Identifiers |
EC number |
3.2.1.25 |
CAS number |
9025-43-8 |
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 / EGO |
Search |
PMC |
articles |
PubMed |
articles |
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 system name beta-D-mannoside mannohydrolase, which is in humans encoded by the MANBA gene.[1][2][3][4][5][6] 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.[1]
References
- ^ 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. and 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. and 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. and 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. and Sawai, K. (1964). "The enzymatic hydrolysis of Leucaena glauca galactomannan. Isolation of crystalline galactomannan depolymerase". J. Biol. Chem. 239: 990–992. PMID 14165949.
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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Index of inborn errors of metabolism
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Description |
- Metabolism
- Enzymes and pathways: citric acid cycle
- pentose phosphate
- glycoproteins
- glycosaminoglycans
- phospholipid
- cholesterol and steroid
- sphingolipids
- eicosanoids
- amino acid
- urea cycle
- nucleotide
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Disorders |
- Citric acid cycle and electron transport chain
- Glycoprotein
- Proteoglycan
- Fatty-acid
- Phospholipid
- Cholesterol and steroid
- Eicosanoid
- Amino acid
- Purine-pyrimidine
- Heme metabolism
- Symptoms and signs
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Treatment |
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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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- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 9
- 10
- 11
- 12
- 13
- 14
- 15-99
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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Proteins: enzymes
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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
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Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
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Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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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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- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 9
- 10
- 11
- 12
- 13
- 14
- 15-99
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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English Journal
- Biochemical characterization of an acidophilic β-mannanase from Gloeophyllum trabeum CBS900.73 with significant transglycosylation activity and feed digesting ability.
- Wang C1, Zhang J2, Wang Y1, Niu C1, Ma R3, Wang Y1, Bai Y1, Luo H4, Yao B5.
- Food chemistry.Food Chem.2016 Apr 15;197(Pt A):474-81. doi: 10.1016/j.foodchem.2015.10.115. Epub 2015 Nov 10.
- Acidophilic β-mannanases have been attracting much attention due to their excellent activity under extreme acidic conditions and significant industrial applications. In this study, a β-mannanase gene of glycoside hydrolase family 5, man5A, was cloned from Gloeophyllum trabeum CBS900.73, and succes
- PMID 26616977
- Metal-dependent thermal stability of recombinant endo-mannanase (ManB-1601) belonging to family GH 26 from Bacillus sp. CFR1601.
- Srivastava PK1, Appu Rao G AR2, Kapoor M3.
- Enzyme and microbial technology.Enzyme Microb Technol.2016 Mar;84:41-9. doi: 10.1016/j.enzmictec.2015.12.010. Epub 2015 Dec 24.
- A GH 26 endo-mannanase from Bacillus sp. CFR1601 was purified to homogeneity (Mw ∼39kDa, specific activity 10,461.5±100IU/mg). Endo-mannanase gene (manb-1601, 1083bp, accession No. KM404299) was expressed in Escherichia coli BL21 (DE3) and showed typical fingerprints of α/β proteins in the far-
- PMID 26827773
- Structural, thermal and rheological characterization of modified Dalbergia sissoo gum-A medicinal gum.
- Munir H1, Shahid M2, Anjum F3, Mudgil D4.
- International journal of biological macromolecules.Int J Biol Macromol.2016 Mar;84:236-45. doi: 10.1016/j.ijbiomac.2015.12.001. Epub 2015 Dec 18.
- Dalbergia sissoo gum was purified by ethanol precipitation. The purified gum was modified and hydrolyzed. Gum was modified by performing polyacrylamide grafting and carboxymethylation methods. The hydrolysis was carried out by using mannanase, barium hydroxide and trifluoroacetic acid. The modified
- PMID 26709145
Japanese Journal
- 2P-052 放線菌マンナナーゼが示す分枝オリゴ糖に対する基質認識の分子機構(酵素学,酵素工学,一般講演)
- A Novel β-1,4-mannanase Isolated from Paenibacillus polymyxa KT551
- Distribution of gastropods in a tidal flat in association with digestive enzyme activities
Related Links
- Mannanase is an enzyme that breaks down compounds known as mannanes. It is used foremost as additive in feed that contains soya and maize. ... Function Mannanase is an Enzym, that breaks down compounds known ...
- mannanase (plural mannanases) (biochemistry) Any enzyme that catalyzes the hydrolysis of mannans Retrieved from "https://en.wiktionary.org/w/index.php?title=mannanase&oldid=36442997" Categories: English lemmas Talk ...
Related Pictures
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[★]
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[★]
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- mannanase
- 関
- マンナナーゼ