NEU1

From Wikipedia, the free encyclopedia
Sialidase 1 (lysosomal sialidase)

Crystallographic structure of influenza A N9 neuraminidase and its complex with the inhibitor 2-deoxy 2,3-dehydro-N-acetyl neuraminic acid.[1]
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsNEU1; NANH; NEU; SIAL1
External IDsOMIM: 608272 MGI: 97305 HomoloGene: 375 ChEMBL: 2726 GeneCards: NEU1 Gene
EC number3.2.1.18
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez475818010
EnsemblENSG00000184494ENSMUSG00000007038
UniProtQ99519O35657
RefSeq (mRNA)NM_000434.3NM_010893.3
RefSeq (protein)NP_000425.1NP_035023.3
Location (UCSC)Chr 6:
31.83 – 31.83 Mb		Chr 17:
35.07 – 35.07 Mb
PubMed search
This box:

Sialidase 1 (lysosomal sialidase), also known as NEU1 is a mammalian lysosomal neuraminidase enzyme which in humans is encoded by the NEU1 gene.[2][3]

Function

The protein encoded by this gene encodes the lysosomal enzyme, which cleaves terminal sialic acid residues from substrates such as glycoproteins and glycolipids. In the lysosome, this enzyme is part of a heterotrimeric complex together with beta-galactosidase and cathepsin A (the latter also referred to as 'protective protein'). Mutations in this gene can lead to sialidosis.[2]

Clinical significance

Deficiencies in the human enzyme NEU1 leads to sialidosis, a rare lysosomal storage disease.[4] Sialidase has also been shown to enhance recovery from spinal cord contusion injury when injected in rats.[5]

Interactions

NEU1 has been shown to interact with Cathepsin A.[6]

References

  1. ↑ PDB 1nna; Bossart-Whitaker P, Carson M, Babu YS, Smith CD, Laver WG, Air GM (August 1993). "Three-dimensional structure of influenza A N9 neuraminidase and its complex with the inhibitor 2-deoxy 2,3-dehydro-N-acetyl neuraminic acid". J. Mol. Biol. 232 (4): 1069–83. doi:10.1006/jmbi.1993.1461. PMID 8371267. 
  2. ↑ 2.0 2.1 "Entrez Gene: NEU1 sialidase 1 (lysosomal sialidase)". 
  3. ↑ Pshezhetsky AV, Richard C, Michaud L, Igdoura S, Wang S, Elsliger MA, Qu J, Leclerc D, Gravel R, Dallaire L, Potier M (March 1997). "Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis". Nat. Genet. 15 (3): 316–20. doi:10.1038/ng0397-316. PMID 9054950. 
  4. ↑ Seyrantepe V, Poupetova H, Froissart R, Zabot MT, Maire I, Pshezhetsky AV (November 2003). "Molecular pathology of NEU1 gene in sialidosis". Hum. Mutat. 22 (5): 343–52. doi:10.1002/humu.10268. PMID 14517945. 
  5. ↑ Mountney A, Zahner MR, Lorenzini I, Oudega M, Schramm LP, Schnaar RL (June 2010). "Sialidase enhances recovery from spinal cord contusion injury". PNAS 22 (5): 343–52. doi:10.1073/pnas.1006683107. PMC 2895144. PMID 20534525. 
  6. ↑ van der Spoel, A; Bonten E, d'Azzo A (Mar 1998). "Transport of human lysosomal neuraminidase to mature lysosomes requires protective protein/cathepsin A". EMBO J. (ENGLAND) 17 (6): 1588–97. doi:10.1093/emboj/17.6.1588. ISSN 0261-4189. PMC 1170506. PMID 9501080. 

Further reading

  • Okamura-Oho Y, Zhang S, Callahan JW (1994). "The biochemistry and clinical features of galactosialidosis". Biochim. Biophys. Acta 1225 (3): 244–54. PMID 8312369.  *Seyrantepe V, Poupetova H, Froissart R, et al. (2004). "Molecular pathology of NEU1 gene in sialidosis". Hum. Mutat. 22 (5): 343–52. doi:10.1002/humu.10268. PMID 14517945. 
  • Verheijen FW, Palmeri S, Galjaard H (1987). "Purification and partial characterization of lysosomal neuraminidase from human placenta". Eur. J. Biochem. 162 (1): 63–7. doi:10.1111/j.1432-1033.1987.tb10542.x. PMID 3102233. 
  • Verheijen FW, Palmeri S, Hoogeveen AT, Galjaard H (1985). "Human placental neuraminidase. Activation, stabilization and association with beta-galactosidase and its protective protein". Eur. J. Biochem. 149 (2): 315–21. doi:10.1111/j.1432-1033.1985.tb08928.x. PMID 3922758. 
  • 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. 
  • Pshezhetsky AV, Potier M (1996). "Association of N-acetylgalactosamine-6-sulfate sulfatase with the multienzyme lysosomal complex of beta-galactosidase, cathepsin A, and neuraminidase. Possible implication for intralysosomal catabolism of keratan sulfate". J. Biol. Chem. 271 (45): 28359–65. doi:10.1074/jbc.271.45.28359. PMID 8910459. 
  • Bonten E, van der Spoel A, Fornerod M, et al. (1997). "Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis". Genes Dev. 10 (24): 3156–69. doi:10.1101/gad.10.24.3156. PMID 8985184.  *Milner CM, Smith SV, Carrillo MB, et al. (1997). "Identification of a sialidase encoded in the human major histocompatibility complex". J. Biol. Chem. 272 (7): 4549–58. doi:10.1074/jbc.272.7.4549. PMID 9020182. 
  • Pshezhetsky AV, Richard C, Michaud L, et al. (1997). "Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis". Nat. Genet. 15 (3): 316–20. doi:10.1038/ng0397-316. PMID 9054950. 
  • Vinogradova MV, Michaud L, Mezentsev AV, et al. (1998). "Molecular mechanism of lysosomal sialidase deficiency in galactosialidosis involves its rapid degradation". Biochem. J. 330 ( Pt 2) (Pt 2): 641–50. PMC 1219185. PMID 9480870. 
  • van der Spoel A, Bonten E, d'Azzo A (1998). "Transport of human lysosomal neuraminidase to mature lysosomes requires protective protein/cathepsin A". EMBO J. 17 (6): 1588–97. doi:10.1093/emboj/17.6.1588. PMC 1170506. PMID 9501080. 
  • Lukong KE, Elsliger MA, Chang Y, et al. (2000). "Characterization of the sialidase molecular defects in sialidosis patients suggests the structural organization of the lysosomal multienzyme complex". Hum. Mol. Genet. 9 (7): 1075–85. doi:10.1093/hmg/9.7.1075. PMID 10767332. 
  • Naganawa Y, Itoh K, Shimmoto M, et al. (2000). "Molecular and structural studies of Japanese patients with sialidosis type 1". J. Hum. Genet. 45 (4): 241–9. doi:10.1007/s100380070034. PMID 10944856. 
  • Bonten EJ, Arts WF, Beck M, et al. (2000). "Novel mutations in lysosomal neuraminidase identify functional domains and determine clinical severity in sialidosis". Hum. Mol. Genet. 9 (18): 2715–25. doi:10.1093/hmg/9.18.2715. PMID 11063730. 
  • Lukong KE, Landry K, Elsliger MA, et al. (2001). "Mutations in sialidosis impair sialidase binding to the lysosomal multienzyme complex". J. Biol. Chem. 276 (20): 17286–90. doi:10.1074/jbc.M100460200. PMID 11279074. 
  • Penzel R, Uhl J, Kopitz J, et al. (2001). "Splice donor site mutation in the lysosomal neuraminidase gene causing exon skipping and complete loss of enzyme activity in a sialidosis patient". FEBS Lett. 501 (2–3): 135–8. doi:10.1016/S0014-5793(01)02645-X. PMID 11470272.  *Lukong KE, Seyrantepe V, Landry K, et al. (2002). "Intracellular distribution of lysosomal sialidase is controlled by the internalization signal in its cytoplasmic tail". J. Biol. Chem. 276 (49): 46172–81. doi:10.1074/jbc.M104547200. PMID 11571282. 
  • Sergi C, Penzel R, Uhl J, et al. (2001). "Prenatal diagnosis and fetal pathology in a Turkish family harboring a novel nonsense mutation in the lysosomal alpha-N-acetyl-neuraminidase (sialidase) gene". Hum. Genet. 109 (4): 421–8. doi:10.1007/s004390100592. PMID 11702224. 
  • Itoh K, Naganawa Y, Matsuzawa F, et al. (2002). "Novel missense mutations in the human lysosomal sialidase gene in sialidosis patients and prediction of structural alterations of mutant enzymes". J. Hum. Genet. 47 (1): 29–37. doi:10.1007/s10038-002-8652-7. PMID 11829139. 
Hydrolase: sugar hydrolases (EC 3.2)
3.2.1: Glycoside hydrolases
Disaccharidase
Glucosidases
Other
3.2.2: Hydrolysing
N-Glycosyl compounds
  • B
  • enzm
  • 1.1
    • 2
    • 3
    • 4
    • 5
    • 6
    • 7
    • 8
    • 10
    • 11
    • 13
    • 14
    • 15-18
  • 2.1
    • 2
    • 3
    • 4
    • 5
    • 6
    • 7
      • 2.7.10
      • 11-12
    • 8
  • 3.1
      • 3.1.3.48
    • 2
    • 3
    • 4
      • 3.4.21
      • 22
      • 23
      • 24
    • 5
    • 6
    • 7
  • 4.1
    • 2
    • 3
    • 4
    • 5
    • 6
  • 5.1
    • 2
    • 3
    • 4
    • 99
  • 6.1-3
    • 4
    • 5-6
This article is issued from Wikipedia. The text is available under the Creative Commons Attribution/Share Alike; additional terms may apply for the media files.