Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.4.23.B5: murine leukemia virus protease

This is an abbreviated version!
For detailed information about murine leukemia virus protease, go to the full flat file.

Word Map on EC 3.4.23.B5

Reaction

processing of viral polyprotein. The retroviral protease is essential for virus replication, by processing of viral Gag and Gag-Pol polyproteins =

Synonyms

MLV PR, MLV protease, MLV retropepsin, MMLV protease, Mo-MuLV PR, Mo-MuLV protease, Moloney MLV retropepsin, Moloney murine leukemia virus protease, Moloney murine leukemia virus retropepsin, More, MuLV 4070A, MuLV proteinase, murine leukemia virus protease, viral protease, vPR

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.B5 murine leukemia virus protease

Engineering

Engineering on EC 3.4.23.B5 - murine leukemia virus protease

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A57I
-
mutation has a strong influence on substrate specificity
C88T
-
mutant enzyme shows an increased preference for hydrophobic amino acids at P4 and P2 position in a series of VSQNYPIVQ analogs
E15R
-
mutant enzyme shows similar kinetic parameters to that of the mutant enzyme
G541R
-
size exclusion chromatography shows that the multimerization properties are similar among expressed wild-type and mutant ectodomain peptides. Circular dichroism measurements reveal decreased thermal stability of the G541R mutant as compared to wild-type. The G541R mutant also renders the peptide more susceptible to Lys-C protease cleavage. A monoclonal antibody does not bind to the G541R mutant peptide, suggesting a structural difference from wild-type
G60F
-
mutant enzyme shows an increased preference for hydrophobic amino acids at P4 and P2 position in a series of VSQNYPIVQ analogs
H37D
-
mutation has a strong influence on substrate specificity
V39I/V54I
-
mutant enzyme shows similar kinetic parameters to that of the mutant enzyme
W53I
-
mutant enzyme shows an increased preference for hydrophobic amino acids at P4 and P2 position in a series of VSQNYPIVQ analogs
W53I/Q55G
-
mutant enzyme does not cleave the wild-type substrates: VSQNYPIVQ, VIQNYPIVQ and VSQNYPLVQ
A57V
99.7% of wild-type activity, 26.6% residual activity in presence of 1 microM amprenavir
K61L
10.3% of wild-type activity, 95% residual activity in presence of 1 microM amprenavir
V39I
23.5% of wild-type activity, 53% residual activity in presence of 1 microM amprenavir
V39I/A57V
27% of wild-type activity, no residual activity in presence of 1 microM amprenavir
Y90A/L92V
15.6% of wild-type activity, 81.7% residual activity in presence of 1 microM amprenavir
additional information