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Literature summary for 3.4.23.B5 extracted from

  • Menendez-Arias, L.; Tozser, J.; Oroszlan, S.
    Moloney murine leukemia virus retropepsin (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ), 1, 176-178.
No PubMed abstract available
Search for more literature for 3.4.23.B5

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli fused to TrpE or to glutathione S-transferase from Schistosoma japonicum Moloney murine leukemia virus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic analysis Moloney murine leukemia virus
0.261
-
 VSQNYPIVQ
-
 Moloney murine leukemia virus

Metals/Ions

Metals/Ions Comment Organism Structure
NaCl activates, optimal at 3 M Moloney murine leukemia virus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
13315
-
 2 * 13315, sequence calculation, homodimer, structure molecular modeling Moloney murine leukemia virus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Gag polyprotein + H2O Moloney murine leukemia virus processing to mature proteins, autolysis of the retropepsin ?
-
 ?
Gag-Pol polyprotein + H2O Moloney murine leukemia virus processing to mature proteins, autolysis of the retropepsin ?
-
 ?

Organism

Organism UniProt Comment Textmining
Moloney murine leukemia virus
-
 Moloney MLV
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the enzyme performs autolytic processing of precursor protein Moloney murine leukemia virus

Purification (Commentary)

Purification (Comment) Organism
native enzyme partially, recombinant enzyme to homogeneity from Escherichia coli Moloney murine leukemia virus

Reaction

Reaction Comment Organism Reaction ID
processing of viral polyprotein. The retroviral protease is essential for virus replication, by processing of viral Gag and Gag-Pol polyproteins substrate binding pocket residues are His37, Val39, and Ala57 Moloney murine leukemia virus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gag polyprotein + H2O
-
 Moloney murine leukemia virus ?
-
 ?
Gag polyprotein + H2O processing to mature proteins, autolysis of the retropepsin Moloney murine leukemia virus ?
-
 ?
Gag-Pol polyprotein + H2O
-
 Moloney murine leukemia virus ?
-
 ?
Gag-Pol polyprotein + H2O processing to mature proteins, autolysis of the retropepsin Moloney murine leukemia virus ?
-
 ?
additional information cleavage site and substrate specificity, overview Moloney murine leukemia virus ?
-
 ?
VSQNYPIVQ + H2O a HIV-1 retropepsin substrate Moloney murine leukemia virus VSQNY + PIVQ
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 13315, sequence calculation, homodimer, structure molecular modeling Moloney murine leukemia virus

Synonyms

Synonyms Comment Organism
MLV protease
-
 Moloney murine leukemia virus
MLV retropepsin
-
 Moloney murine leukemia virus
Moloney MLV retropepsin
-
 Moloney murine leukemia virus
Moloney murine leukemia virus retropepsin
-
 Moloney murine leukemia virus
More the enzyme belongs to the A2 peptidase family Moloney murine leukemia virus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
 Moloney murine leukemia virus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.55
-
 VSQNYPIVQ pH 6.0, 37°C Moloney murine leukemia virus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Moloney murine leukemia virus