3.4.23.B11: spumapepsin

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For detailed information about spumapepsin, go to the full flat file.

Reaction

Good cleavage at the peptide bonds: Asn-Thr, Asn-Gln, Asn-Cys and Asn-Ala =

Synonyms

core polyprotein, Gag polyprotein, HFV PR, HSRV protease, human foamy virus protease, human foamy virus protease PR, human foamy virus proteinase, More, spumapepsin

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.23 Aspartic endopeptidases

                3.4.23.B11 spumapepsin

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Results	in table
2	Activating Compound
3	AA Sequence
1	CAS Registry Number
8	Cloned(Commentary)
2	General Information
2	General Stability
3	IC50 Value
3	Inhibitors
12	KM Value [mM]
5	Molecular Weight [Da]
7	Natural Substrates/ Products (Substrates)
20	Organism
9	pH Optimum
2	pH Range
1	pH Stability
8	Protein Variants
3	Purification (Commentary)
1	Reaction
20	Reference
1	Renatured (Commentary)
2	Specific Activity [micromol/min/mg]
39	Substrates and Products (Substrate)
11	Subunits
21	Synonyms
2	Temperature Optimum [°C]
10	Turnover Number [1/s]

Activating Compound

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Activating Compound on EC 3.4.23.B11 - spumapepsin

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ACTIVATING COMPOUND

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

NaCl

Simian foamy virus

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assay at 3 M, no activity at salt concentrations of 0.2-0.4 M Na. In vitro dimerization of the protease domain is inducible at high salt concentrations. This effect might be caused by a hydrophobic dimerization interface, which under high ionic strength disfavors the monomeric state

718389

additional information

Simian foamy virus

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identification of a specific protease-activating RNA motif PARM located in the pol region of viral RNA, which stimulates protease activity in vitro and in vivo. PARM spans the A and B regions of the central purine-rich sequences of the prototype foamy virus (pre)genomic RNA. PARM enables foamy virus protease-reverse transcriptase to form a proteolytically active dimer in vitro as well as in vivo. At least two foamy virus protease-reverse transcriptase molecules bind to the PARM and only RNAs containing the PARM result in significant activation of the protease. DNA harboring the PARM is not capable of protease activation.The PARM displays a distinct RNA folding, important for protease activation and thus virus maturation

718058

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