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3.4.23.B2: Simian immunodeficiency virus proteinase

This is an abbreviated version!
For detailed information about Simian immunodeficiency virus proteinase, go to the full flat file.

Word Map on EC 3.4.23.B2

Reaction

The enzyme may have a wide substrate specificity. Good cleavage of the peptide bonds Met-Met and Tyr-Pro. Cleavage is also observed at Phe-Pro, Phe-Leu, Leu-Phe, Leu-Ala, Glu-Ala and Tyr-Ala =

Synonyms

More, Pol polyprotein, retropepsin, Simian immunodeficiency virus protease, simian immunodeficiency virus retropepsin, SIV PR, SIV protease, SIV proteinase, SIV retropepsin, SIV-PR

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.B2 Simian immunodeficiency virus proteinase

Natural Substrates Products

Natural Substrates Products on EC 3.4.23.B2 - Simian immunodeficiency virus proteinase

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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Pr55Gag polyprotein + H2O
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show the reaction diagram
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lentiviral Gag polyprotein, proteolytic processing for activation, cleavage in the late stages of life cycle, required for maturation of the virion meaning a structural rearrangement required for infectivity in budding virions, cleavage in the phosphorylated capsid domains, the enzyme is not influenced by the preceeding phosphorylation, but cleaved sites are no longer phosphorylated, while incompletely cleaved capsid domains are phosphorylated to a greater extent, overview
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