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Literature summary for 3.4.22.44 extracted from

  • Han, H.E.; Sellamuthu, S.; Shin, B.H.; Lee, Y.J.; Song, S.; Seo, J.S.; Baek, I.S.; Bae, J.; Kim, H.; Yoo, Y.J.; Jung, Y.K.; Song, W.K.; Han, P.L.; Park, W.J.
    The nuclear inclusion a (NIa) protease of turnip mosaic virus (TuMV) cleaves amyloid-beta (2010), PLoS ONE, 5, e15645.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
cloning of NIa in Escherichia coli, overexpression of HA-tagged NIa in rat B103 neuroblastoma cells turnip mosaic virus

Protein Variants

Protein Variants Comment Organism
additional information overexpression of HA-tagged NIa in rat B103 neuroblastoma cells and lentiviral-mediated expression of NIa in APPsw/PS1 transgenic mice or human 293T cells, the pattern of NIa expression shows a wide distribution throughout the mouse brain including the cerebral cortex, hippocampus, amygdala, and thalamus, and the Amyloid-beta deposition in the prefrontal cortex, parietal cortex, hippocampus and piriform cortex is remarkably decreased in the brain infused with Lenti-NIa in comparison to the brain infused with Lenti-GFP. Expression of wild-type and utant, with an Asp to Ala substitution in the catalytic triad,.Amyloid-beta intracellularly in B103 cells using the plasmid pGFPUb-Abeta, encoding a triple fusion protein of green fluorescent protein, ubiquitin, and Amylod-beta. The peptide bond between ubiquitin and Amyloid-beta is cleaved quickly by endogenous deubiquitinating enzymes, generating an equimolar ratio of GFP-ubiquitin and Amyloid-beta in the cytosol turnip mosaic virus

Inhibitors

Inhibitors Comment Organism Structure
NEM does not completely inhibit NIa activity turnip mosaic virus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol predominantly turnip mosaic virus 5829
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Organism

Organism UniProt Comment Textmining
turnip mosaic virus
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TuMV
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amyloid-beta peptide + H2O degradation of oligomeric as well as monomeric forms of Amyloid-beta, presence of the consensus sequence, Val12-His-His-Gln15, near the presumptive alpha-secretase cleavage site of the amyloid-beta peptide turnip mosaic virus ?
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?
additional information NIa possesses a relatively strict substrate specificity with a preference for Val-Xaa-His-GlnQ, with the scissile bond located after Gln turnip mosaic virus ?
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?

Synonyms

Synonyms Comment Organism
NIa protease
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turnip mosaic virus
nuclear inclusion a protease
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turnip mosaic virus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at turnip mosaic virus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at turnip mosaic virus

General Information

General Information Comment Organism
additional information overexpression of NIa in rat B103 neuroblastoma cells results in a significant reduction in cell death caused by both intracellularly generated and exogenously added Amyloidbeta. Moreover, lentiviral-mediated expression of NIa in APPsw/PS1 transgenic mice significantly reduces the levels of Amyloid-beta and plaques in the brain turnip mosaic virus
physiological function the nuclear inclusion a protease of turnip mosaic virus is responsible for the processing of the viral polyprotein into functional proteins. Degradation of Amyloid-beta in the cytoplasm can be a novel strategy to control the levels of Amyloid-beta, plaque formation, and the associated cell death turnip mosaic virus