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Literature summary for 3.4.23.B5 extracted from

  • Bagossi, P.; Sperka, T.; Feher, A.; Kadas, J.; Zahuczky, G.; Miklossy, G.; Boross, P.; Toezser, J.
    Amino acid preferences for a critical substrate binding subsite of retroviral proteases in type 1 cleavage sites (2005), J. Virol., 79, 4213-4218.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.23.B5

Cloned(Commentary)

Cloned (Comment) Organism
expression as His-tagged maltose-binding protein fusion enzyme in Escherichia coli, phylogenetic tree Moloney murine leukemia virus

Organism

Organism UniProt Comment Textmining
Moloney murine leukemia virus
-
 MMLV, belongs to the gamma-retrovirus group
-

Purification (Commentary)

Purification (Comment) Organism
expression as His-tagged maltose-binding protein fusion enzyme from Escherichia coli, the fusion protein is cleaved off 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 structure-based molecular modeling of reaction mechanism and substrate binding Moloney murine leukemia virus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information study of influence of the P2 position residue on cleavage site specificity, overview Moloney murine leukemia virus ?
-
 ?
Val-Ser-Gln-Ala-Tyr-Pro-Ile-Val-Gln + H2O
-
 Moloney murine leukemia virus Val-Ser-Gln-Ala-Tyr + Pro-Ile-Val-Gln
-
 ?
Val-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln + H2O
-
 Moloney murine leukemia virus Val-Ser-Gln-Asn-Tyr + Pro-Ile-Val-Gln
-
 ?
Val-Ser-Gln-Cys-Tyr-Pro-Ile-Val-Gln + H2O
-
 Moloney murine leukemia virus Val-Ser-Gln-Cys-Tyr + Pro-Ile-Val-Gln
-
 ?
Val-Ser-Gln-Gly-Tyr-Pro-Ile-Val-Gln + H2O
-
 Moloney murine leukemia virus Val-Ser-Gln-Gly-Tyr + Pro-Ile-Val-Gln
-
 ?
Val-Ser-Gln-Ile-Tyr-Pro-Ile-Val-Gln + H2O
-
 Moloney murine leukemia virus Val-Ser-Gln-Ile-Tyr + Pro-Ile-Val-Gln
-
 ?
Val-Ser-Gln-Leu-Tyr-Pro-Ile-Val-Gln + H2O
-
 Moloney murine leukemia virus Val-Ser-Gln-Leu-Tyr + Pro-Ile-Val-Gln
-
 ?
Val-Ser-Gln-Phe-Tyr-Pro-Ile-Val-Gln + H2O
-
 Moloney murine leukemia virus Val-Ser-Gln-Phe-Tyr + Pro-Ile-Val-Gln
-
 ?
Val-Ser-Gln-Thr-Tyr-Pro-Ile-Val-Gln + H2O
-
 Moloney murine leukemia virus Val-Ser-Gln-Thr-Tyr + Pro-Ile-Val-Gln
-
 ?
Val-Ser-Gln-Val-Tyr-Pro-Ile-Val-Gln + H2O
-
 Moloney murine leukemia virus Val-Ser-Gln-Val-Tyr + Pro-Ile-Val-Gln
-
 ?

Subunits

Subunits Comment Organism
More structure molecular modeling, S2 subsite sequence comparison Moloney murine leukemia virus

Synonyms

Synonyms Comment Organism
MMLV protease
-
 Moloney murine leukemia virus

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.6
-
 assay at Moloney murine leukemia virus