3.4.23.50: human endogenous retrovirus K endopeptidase
This is an abbreviated version!
For detailed information about human endogenous retrovirus K endopeptidase, go to the full flat file.
Reaction
Processing at the authentic HIV-1 PR recognition site and release of the mature p17 matrix and the p24 capsid protein, as a result of the cleavage of the -SQNY-/-PIVQ- cleavage site. =
Synonyms
endogenous retrovirus encoded protease, endogenous retrovirus HERV-K10 putative protease, HERV K10 endopeptidase, HERV K10 retropepsin, HERV-K PR, HERV-K protease, HERV-K(HML-2) Pro, HERV-K(HML-2) protease, HERV-K113 protease, HML-2 Pro, human endogenous retrovirus K retropepsin, human endogenous retrovirus K113 protease, human retrovirus K10 retropepsin, More
ECTree
3.4.23.50 human endogenous retrovirus K endopeptidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.23.50 - human endogenous retrovirus K endopeptidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-Ala-Thr-His-Gln-Val-Tyr-Phe(NO2)-Val-Arg-Lys-Ala + H2O
?
-
-
-
-
?
2-aminobenzoyl-ATHQVY-(4-nitro)FVRKA + H2O
2-aminobenzoyl-ATHQVY + (4-nitro)FVRKA
-
-
-
-
?
Gag polyprotein + H2O
?
-
the enzyme is synthesized as part of the Gag polyprotein or the Gag-Pol polyprotein and autolytically processed to the mature dimer
-
-
?
Gag-Pol polyprotein + H2O
?
-
the enzyme is synthesized as part of the Gag polyprotein or the Gag-Pol polyprotein and autolytically processed to the mature dimer
-
-
?
HERV-K Gag polyprotein + H2O
?
-
processing of HERV-K Gag is dependent on the presence of the functional retroviral protease
HERV-K Gag is processed into matrix protein, a short spacer peptide, p15, capsid and nucelocapsid
-
?
HIV-1 matrix-capsid polyprotein + H2O
?
-
processing at the authentic HIV-1 PR recognition site
-
-
?
HIV-1 matrix-capsid polyprotein + H2O
?
-
cleavage also in presence of HIV-1 PR inhibitor
-
-
?
additional information
?
-
-
the results do not exclude the possibility that the HERV-K PR could complement an HIV-1 PR whoses function is impaired due to drugs or drug-resistant mutations, they clearly demomstrate that the HERV-K PR cannot substitute for the function of the wild-type HIV-1 PR
-
-
?
additional information
?
-
-
the enzyme probably functions in the processing of Gag precursor protein
-
-
?
additional information
?
-
-
the C-terminal 13-amino-acid extension of the enzyme might play a regulatory role
-
-
?
additional information
?
-
-
the N-terminal cleavage site for HERV-K capsid protein matches the sequence consistently found at the N-terminus of all retroviral capsid proteins. The other cleavage sites correspond well to the simplified version of a cleavage site as an amino acid stretch that is hydrophobic and both accessible and flexible, i.e. apparently the space between separately folded domainsof Gag
-
-
?
additional information
?
-
-
hundreds of cellular proteins are potential substrates of enzyme HERV-K(HML-2) Pro
-
-
?
additional information
?
-
-
identification of human cellular proteins that are substrates of HERV-K(HML-2) Pro employing a modified Terminal Amine Isotopic Labeling of Substrates (TAILS) procedure. Confirmation of cleavage of a majority of selected human proteins in vitro and in co-expression experiments in vivo, overview
-
-
?
