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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

Cloned

Cloned on EC 3.4.23.B2 - Simian immunodeficiency virus proteinase

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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned directly from proviral DNA of the infectious viral stock SIVmac251-32H(11/88 pool). SIVmac251-32H proteinase and ist flanking pol sequences are expressed in Escherichia coli as a fusion protein with most of the T7 bacteriophage gene 10 protein. The expressed protein forms cytoplasmic inclusion bodies which are solubilized in 8 M urea, and the recombinant enzyme is refolded, yielding active self-processing enzyme
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expressed in Escherichia coli with a recombinant expression system
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expression in Escherichia coli
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expression in Escherichia coli, expression as N-terminally capped, biotin-labeled precursor
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