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Literature summary for 3.4.23.47 extracted from

  • Alvarez, E.; Castello, A.; Menendez-Arias, L.; Carrasco, L.
    HIV protease cleaves poly(A)-binding protein (2006), Biochem. J., 396, 219-226.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.23.47

Activating Compound

Activating Compound Comment Organism Structure
DTT
-
 Human immunodeficiency virus 2
EDTA
-
 Human immunodeficiency virus 2

Application

Application Comment Organism
medicine the poly(A)-binding protein is known to be cleaved by several picornaviruses and caliciviruses. The results indicate that retroviruses such as HIV share the capacity to proteolyse poly(A)-binding protein Human immunodeficiency virus 2

Cloned(Commentary)

Cloned (Comment) Organism
BHK-21 (baby hamster kidney) cells and COS-7 cells are transfected with HIV-1 and HIV-2 protease and human poly(A)-binding protein 1 Human immunodeficiency virus 2

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 2
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
poly(A)-binding protein 1 + H2O it is shown that HIV-1 and HIV-2 protease cleaves poly(A)-binding protein 1 directly at positions 237 and 477, separating the two first RNA-recognition motifs from the C-terminal domain of poly(A)-binding protein and additional cleavage site at position 410 is detected for HIV2-protease Human immunodeficiency virus 2 ?
-
 ?

Synonyms

Synonyms Comment Organism
HIV-2 protease
-
 Human immunodeficiency virus 2

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Human immunodeficiency virus 2

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 assay at Human immunodeficiency virus 2