3.4.23.16: HIV-1 retropepsin
This is an abbreviated version!
For detailed information about HIV-1 retropepsin, go to the full flat file.
Word Map on EC 3.4.23.16
-
3.4.23.16
-
antiretroviral
-
ritonavir
-
transcriptase
-
saquinavir
-
indinavir
-
nelfinavir
-
hiv-infected
-
lopinavir
-
polyproteins
-
flap
-
darunavir
-
amprenavir
-
drug-resistant
-
anti-hiv
-
atazanavir
-
virological
-
haart
-
gag-pol
-
peptidomimetic
-
virion
-
p-glycoprotein
-
lipodystrophy
-
non-nucleoside
-
integrase
-
cross-resistance
-
isostere
-
nonpeptidic
-
zidovudine
-
nevirapine
-
virus-1
-
tipranavir
-
cyp3a4
-
nnrti
-
drug-drug
-
treatment-experienced
-
lamivudine
-
didanosine
-
ritonavir-boosted
-
autoprocessing
-
efavirenz
-
protease-inhibitor
-
stavudine
-
treatment-naive
-
analysis
-
raltegravir
-
zalcitabine
-
plasmepsins
-
antiretroviral-naive
-
pi-based
-
pharmacology
-
drug development
-
medicine
-
hiv-rna
-
lipoatrophy
- 3.4.23.16
-
antiretroviral
- ritonavir
- transcriptase
- saquinavir
- indinavir
- nelfinavir
-
hiv-infected
- lopinavir
- polyproteins
- flap
- darunavir
- amprenavir
-
drug-resistant
-
anti-hiv
- atazanavir
-
virological
-
haart
- gag-pol
-
peptidomimetic
- virion
- p-glycoprotein
- lipodystrophy
-
non-nucleoside
-
integrase
-
cross-resistance
- isostere
-
nonpeptidic
- zidovudine
- nevirapine
- virus-1
- tipranavir
- cyp3a4
-
nnrti
-
drug-drug
-
treatment-experienced
- lamivudine
- didanosine
-
ritonavir-boosted
-
autoprocessing
- efavirenz
-
protease-inhibitor
- stavudine
-
treatment-naive
- analysis
- raltegravir
- zalcitabine
-
plasmepsins
-
antiretroviral-naive
-
pi-based
- pharmacology
- drug development
- medicine
-
hiv-rna
-
lipoatrophy
Reaction
specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro =
Synonyms
CRF01_AE protease, Gag protease, HIV aspartyl protease, HIV PR, HIV protease, HIV-1 aspartyl protease, HIV-1 PR, HIV-1 protease, HIV-1 proteinase, HIV-1PR, HIV-2 protease, HIVPR, human immunodeficiency virus 1 protease, human immunodeficiency virus 1 retropepsin, human immunodeficiency virus protease, human immunodeficiency virus type 1 protease, human immunodeficiency virus type I protease, More, PR, PR1, PR2, retropepsin, retroproteinase
ECTree
3.4.23.16 HIV-1 retropepsinAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.23.16 - HIV-1 retropepsin
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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-Thr-Ile-Nle-4-nitro-Phe-Gln-Arg-NH2 + H2O
2-aminobenzoyl-Thr-Ile-Nle + 4-nitro-Phe-Gln-Arg-NH2
-
-
-
-
?
2-aminobenzoyl-Thr-Ile-Nle-p-nitro-Phe-Gln-Arg-NH2 + H2O
2-aminobenzoyl-Thr-Ile-Nle + p-nitro-Phe-Gln-Arg-NH2
-
-
-
-
?
2-aminobenzoyl-TI-Nle-Phe(NO2)-ER + H2O
2-aminobenzoyl-Thr-Ile-Nle + Phe(NO2)-Glu-Arg
-
-
-
-
?
2-aminobenzoyl-TI-Nle-Phe(NO2)-QR + H2O
2-aminobenzoyl-Thr-Ile-Nle + Phe(NO2)-Gln-Arg
-
-
-
-
?
2-aminobenzoyl-TI-Nle-Phe(NO2)-QR-NH2 + H2O
2-aminobenzoyl-Thr-Ile-Nle + Phe(NO2)-Gln-Arg-NH2
-
the enzyme reacts with the substrate to give an initial enzyme-substrate complex that isomerizes to a kinetically competent intermediate EX
-
-
?
4-(4-(dimethylamino)phenylazo)benzoyl-SQNYPIVQ-5-((2-aminoethyl)amino)naphthalene-1-sulfonic acid + H2O
?
-
-
-
-
?
Abz-Ala-Arg-Val-Nle-(p-nitro)Phe-Phe-Glu-Ala-Nle-NH2 + H2O
Abz-Ala-Arg-Val-Nle + (p-nitro)Phe-Phe-Glu-Ala-Nle-NH2
-
-
-
-
?
Abz-Arg-Val-Nle-(p-nitro)Phe-Phe-Glu-Ala-Nle-NH2 + H2O
Abz-Arg-Val-Nle + (p-nitro)Phe-Phe-Glu-Ala-Nle-NH2
-
-
-
-
?
Abz-KARV-Nle-Phe(NO2)-EA-Nle-NH2 + H2O
Abz-KARV-Nle + Phe(NO2)-EA-Nle-NH2
-
-
-
-
?
Abz-Lys-Ala-Arg-Val-Nle-(p-nitro)Phe-Phe-Glu-Ala-Nle-NH2 + H2O
Abz-Lys-Ala-Arg-Val-Nle + (p-nitro)Phe-Phe-Glu-Ala-Nle-NH2
-
-
-
-
?
Abz-Thr-Ile-Nle-(p-nitro)Phe-Gln-Arg-NH2 + H2O
Abz-Thr-Ile-Nle + (p-nitro)Phe-Gln-Arg-NH2
-
-
-
-
?
Abz-Thr-Ile-Nle-4-nitro-Phe-Gln-Arg-NH2 + H2O
Abz-Thr-Ile-Nle + 4-nitro-Phe-Gln-Arg-NH2
-
the fluorogenic peptide substrate
-
-
?
Abz-Thr-Ile-Nle-Phe(NO2)-Gln-Arg + H2O
Abz-Thr-Ile-Nle + Phe(NO2)-Gln-Arg
-
-
-
-
?
Abz-Thr-Nle-Phe(NO2)-QR-NH2 + H2O
Abz-Thr-Ile-Nle + Phe(NO2)-Gln-Arg-NH2
-
-
-
-
?
Ac-KASQ(p-nitrophenylalanine)PPV-NH2 + H2O
Ac-KASQ + (4-nitro)FPPV-NH2
-
-
-
-
?
acetyl-KDKTK-Abz-VLF-NO2-VQPKK-NH2 + H2O
acetyl-KDKTK-Abz-VL + F-NO2-VQPKK-NH2
-
-
-
?
Arg-Glu(EDANS)-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln Lys-(DABCYL)-Arg + H2O
?
-
-
-
?
Arg-Glu(EDANS)-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-Lys(DABCYL)-Arg + H2O
?
-
-
-
-
?
Arg-Glu-[5-[(2'-aminoethyl)-amino]naphthalenesulfonyl]-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-Lys-[4-[[4'-(dimethylamino)phenyl]azo]-benzoyl]-Arg + H2O
?
-
-
-
-
?
Arg-Pro-Gly-Asn-Phe-Leu-Gln-Ser-Arg-Pro + H2O
?
decameric p1-p6 peptide
-
-
?
ATHDVY-Phe(NO2)-VRKA + H2O
ATHDVY + Phe(NO2)-VRKA
-
-
-
?
ATHNVY-Phe(NO2)-VRKA + H2O
ATHNVY + Phe(NO2)-VRKA
-
-
-
?
ATHQVY-Phe(NO2)-VRKA + H2O
ATHQVY + Phe(NO2)-VRKA
-
-
-
?
ATHRVY-Phe(NO2)-VRKA + H2O
ATHRVY + Phe(NO2)-VRKA
-
-
-
?
ATHVVY-Phe(NO2)-VRKA + H2O
ATHVVY + Phe(NO2)-VRKA
-
-
-
?
ATHYVY-Phe(NO2)-VRKA + H2O
ATHYVY + Phe(NO2)-VRKA
-
-
-
?
beta-secretase + H2O
truncated beta-secretase protein + peptide E25-F39
-
expression of beta-secretase in mammalian host cells leads to full-length pro-form and the processed enzyme missing the first 24 amino acids and beginning with residue E25. Protease treatment of the mixture results in complete cleavage of the F39-V40 bond
-
-
?
beta-secretase precursor protein + H2O
truncated beta-secretase protein + peptide T1-F39
-
expression of beta-secretase in mammalian host cells leads to full-length pro-form and the processed enzyme missing the first 24 amino acids and beginning with residue E25. Protease treatment of the mixture results in complete cleavage of the F39-V40 bond
-
-
?
DABCYL-(gamma-Abu)-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-EDANS + H2O
?
-
-
-
-
?
eIF4GI + H2O
?
-
perhaps cleavage of eIF4G is an event that contributes to a more efficient translation of the genomic HIV-1 mRNA, proteolysis of eIF4GI inhibits protein synthesis directed by capped mRNAs but allows internal ribosome entry site-driven translation, purified enzyme cleaves at positions 678-679, 681-682 and 1086-1087, separating the three domains of the initiation factor
-
-
?
Gag polyprotein + H2O
matrix-capsid polyprotein + ?
Gag polyprotein with cleavage-site P12-P5/P5'-P12' residues
-
-
?
Gag precursor polyprotein + H2O
mature Gag polyprotein + ?
-
-
-
-
?
Gag precursor protein + H2O
?
-
five different cleavage sites, the p2-NC-site is the first, the CA/p2 the last one in sequential processing of the precursor
-
-
?
Gag-Pol precursor polyprotein + H2O
mature Gag-Pol polyprotein + ?
-
-
-
-
?
H-Lys-Ala-Arg-Val-Tyr-Phe(4-NO2)-Glu-Ala-Nle-NH2 + H2O
Lys-Ala-Arg-Val-Tyr + Phe(4-NO2)-Glu-Ala-Nle-NH2
-
-
-
-
?
His-Lys-Ala-Arg-Val-Leu-(4-nitro)Phe-Glu-Ala-Nle-Ser-amide + H2O
His-Lys-Ala-Arg-Val-Leu + (4-nitro)Phe-Glu-Ala-Nle-Ser-amide
-
-
-
-
?
His-Lys-Ala-Arg-Val-Leu-(p-NO2-Phe)-Glu-Ala-Nle-Ser-NH2 + H2O
His-Lys-Ala-Arg-Val-Leu + (p-NO2-Phe)-Glu-Ala-Nle-Ser-NH2
-
-
-
-
?
His-Lys-Ala-Arg-Val-Leu-(pNO2-Phe)-Glu-Ala-Ile-Ser-NH2 + H2O
His-Lys-Ala-Arg-Val-Leu + (pNO2-Phe)-Glu-Ala-Ile-Ser-NH2
-
-
-
-
?
His-Lys-Ala-Arg-Val-Leu-(pNO2-Phe)-Glu-Ala-Nle-Ser-NH2 + H2O
?
-
-
-
-
?
HIV-1 Gag-Pol polyprotein + H2O
?
-
site-specific proteolytic cleavage, protein precursors and peptides derived thereof
-
-
?
HIV-2 Gag-Pol poylprotein + H2O
?
-
site-specific proteolytic cleavage, protein precursors and peptides derived thereof
-
-
?
IPFAAAQQRK + H2O
IPFAA + AQQRK
the protein contains a HIV-2 cleavage site
-
-
?
KARA-Nle-Phe(NO2)-EA-Nle + H2O
KARA-Nle + Phe(NO2)-EA-Nle
-
-
-
?
KARI-Nle-Phe(NO2)-EA-Nle + H2O
KARI-Nle + Phe(NO2)-EA-Nle
-
-
-
?
KARL-Nle-Phe(NO2)-EA-Nle + H2O
KARL-Nle + Phe(NO2)-EA-Nle
-
-
-
?
KARLMAEALK + H2O
KARLM + AEALK
the protein contains a HIV-2 cleavage site
-
-
?
KARN-Nle-Phe(NO2)-EA-Nle + H2O
KARN-Nle + Phe(NO2)-EA-Nle
-
-
-
?
KARV-Nle-Phe(NO2)-AA-Nle + H2O
KARV-Nle + Phe(NO2)-AA-Nle
-
-
-
?
KARV-Nle-Phe(NO2)-IA-Nle + H2O
KARV-Nle + Phe(NO2)-IA-Nle
-
-
-
?
KARV-Nle-Phe(NO2)-NA-Nle + H2O
KARV-Nle + Phe(NO2)-NA-Nle
-
-
-
?
KARV-Nle-Phe(NO2)-QA-Nle + H2O
KARV-Nle + Phe(NO2)-QA-Nle
-
-
-
?
KARV-Nle-Phe(NO2)-TA-Nle + H2O
KARV-Nle + Phe(NO2)-TA-Nle
-
-
-
?
KARV-Nle-Phe(NO2)-VA-Nle + H2O
KARV-Nle + Phe(NO2)-VA-Nle
-
-
-
?
KARVMPhe(NO2)-EA-Nle + H2O
KARVM + Phe(NO2)-EA-Nle
-
-
-
?
KARVYPhe(NO2)-EA-Nle + H2O
KARVY + Phe(NO2)-EA-Nle
-
-
-
?
Lys-Ala-Arg-Val-Leu-4-nitro-Phe-Glu-Ala-Nle-Gly + H2O
Lys-Ala-Arg-Val-Leu + 4-nitro-Phe-Glu-Ala-Nle-Gly
Lys-Ala-Arg-Val-Leu-Ala-Glu-Ala-Met + H2O
?
-
in the protease-substrate complex the highest fluctuations correspond to the 17- and 39-turns and the substrate motion is anticorrelated with the 39-turn. The active site residues and the flap tips move in phase with the peptide
-
-
?
Lys-Ala-Arg-Val-Leu-Phe(NO2)-Glu-Ala-Met + H2O
Lys-Ala-Arg-Val-Leu + Phe(NO2)-Glu-Ala-Met
-
-
-
-
?
Lys-Ala-Arg-Val-Nle-(4-nitrophenylalanine)-Glu-Ala-Nle-NH2 + H2O
Lys-Ala-Arg-Val-Nle + (4-nitrophenylalanine)-Glu-Ala-Nle-NH2
Lys-Ala-Arg-Val-Nle-(p-nitro-Phe)-Glu-Ala-Nle-amide + H2O
Lys-Ala-Arg-Val-Nle + (p-nitro-Phe)-Glu-Ala-Nle-amide
-
-
-
-
?
Lys-Ala-Arg-Val-Nle-4-nitro-Phe-Glu-Ala-Nle-amide + H2O
Lys-Ala-Arg-Val-Nle + 4-nitro-Phe-Glu-Ala-Nle-amide
Lys-Ala-Arg-Val-Nle-Phe(4-NO2)-Glu-Ala-Nle-Gly + H2O
Lys-Ala-Arg-Val-Nle + Phe(4-NO2)-Glu-Ala-Nle-Gly
-
-
-
-
?
Lys-Ala-Arg-Val-Nle-Phe(4-NO2)-Glu-Ala-Nle-NH2 + H2O
Lys-Ala-Arg-Val-Nle + Phe(4-NO2)-Glu-Ala-Nle-NH2
-
-
-
-
?
Lys-Ala-Arg-Val-Tyr-p-nitro-Phe-Glu-Ala-Ile-NH2 + H2O
?
-
-
-
-
?
matrix-capsid polyprotein + H2O
DTGNNSQVSQNY + PIVQNLQGQMVH
i.e. DTGNNSQVSQNYPIVQNLQGQMVH
-
-
?
Moloney murine sarcoma virus-derived gag protein + H2O
?
-
-
-
-
?
Val-Ser-Gln-Ala-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Ala-Tyr + Pro-Ile-Val-Gln
-
-
-
?
Val-Ser-Gln-Asn-(2-naphthylalanine)-Pro-Ile-Val + H2O
?
-
-
-
-
?
Val-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Asn-Tyr + Pro-Ile-Val-Gln
-
-
-
?
Val-Ser-Gln-Cys-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Cys-Tyr + Pro-Ile-Val-Gln
-
-
-
?
Val-Ser-Gln-Gly-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Gly-Tyr + Pro-Ile-Val-Gln
-
-
-
?
Val-Ser-Gln-Ile-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Ile-Tyr + Pro-Ile-Val-Gln
-
-
-
?
Val-Ser-Gln-Leu-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Leu-Tyr + Pro-Ile-Val-Gln
-
-
-
?
Val-Ser-Gln-Phe-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Phe-Tyr + Pro-Ile-Val-Gln
-
-
-
?
Val-Ser-Gln-Thr-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Thr-Tyr + Pro-Ile-Val-Gln
-
-
-
?
Val-Ser-Gln-Val-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Val-Tyr + Pro-Ile-Val-Gln
-
-
-
?
VSQLYPIVQ + H2O
VSQLY + PIVQ
the protein contains a HIV-1 cleavage site
-
-
?
VSQVYPIVQ + H2O
VSQVY + PIVQ
the protein contains a HIV-1 cleavage site
-
-
?
YVSQNFPIVQNR + H2O
YVSQNF + PIVQNR
-
synthetic peptide substrate based on the Ma/Ca cleavage site of HIV-1 Gag
-
-
?
Gag polyprotein + H2O
?
-
-
-
-
?
Gag polyprotein + H2O
?
-
CA/p2 cleavage site is KARVL*AEAMS
-
-
?
Gag protein + H2O
?
-
proteolytic cleavage in the host cell cytoplasm
-
-
?
Gag protein + H2O
?
-
site-specific proteolytic cleavage of the protein precursor
-
-
?
Gag-Pol polyprotein + H2O
?
-
-
-
-
?
Gag-Pol polyprotein + H2O
?
-
proteolytic cleavage in the host cell cytoplasm
-
-
?
Gag-Pol polyprotein + H2O
?
-
NC/p1 cleavage site is ERQAN*FLGKI
-
-
?
Gag-Pol polyprotein + H2O
?
-
site-specific proteolytic cleavage of the protein precursor
-
-
?
KARV-Nle-Phe(NO2)-EA-Nle + H2O
KARV-Nle + Phe(NO2)-EA-Nle
-
-
-
?
KARV-Nle-Phe(NO2)-EA-Nle + H2O
KARV-Nle + Phe(NO2)-EA-Nle
-
-
-
-
?
KARV-Nle-Phe(NO2)-EA-Nle-NH2 + H2O
KARV-Nle + Phe(NO2)-EA-Nle-NH2
-
-
-
-
?
KARV-Nle-Phe(NO2)-EA-Nle-NH2 + H2O
KARV-Nle + Phe(NO2)-EA-Nle-NH2
-
-
-
?
KARV-Nle-Phe(NO2)-EA-Nle-NH2 + H2O
KARV-Nle + Phe(NO2)-EA-Nle-NH2
-
-
-
?
Lys-Ala-Arg-Val-Leu-4-nitro-Phe-Glu-Ala-Nle-Gly + H2O
Lys-Ala-Arg-Val-Leu + 4-nitro-Phe-Glu-Ala-Nle-Gly
-
i.e. substrate L6525, the peptide substrate contains the CA-p2 cleavage site
-
-
?
Lys-Ala-Arg-Val-Leu-4-nitro-Phe-Glu-Ala-Nle-Gly + H2O
Lys-Ala-Arg-Val-Leu + 4-nitro-Phe-Glu-Ala-Nle-Gly
-
the peptide substrate mimicks the CA-p2 cleavage site
-
-
?
Lys-Ala-Arg-Val-Nle-(4-nitrophenylalanine)-Glu-Ala-Nle-NH2 + H2O
Lys-Ala-Arg-Val-Nle + (4-nitrophenylalanine)-Glu-Ala-Nle-NH2
-
-
-
-
?
Lys-Ala-Arg-Val-Nle-(4-nitrophenylalanine)-Glu-Ala-Nle-NH2 + H2O
Lys-Ala-Arg-Val-Nle + (4-nitrophenylalanine)-Glu-Ala-Nle-NH2
-
-
-
?
Lys-Ala-Arg-Val-Nle-4-nitro-Phe-Glu-Ala-Nle-amide + H2O
Lys-Ala-Arg-Val-Nle + 4-nitro-Phe-Glu-Ala-Nle-amide
-
the peptide substrate mimicks the CA-p2 cleavage site
-
-
?
Lys-Ala-Arg-Val-Nle-4-nitro-Phe-Glu-Ala-Nle-amide + H2O
Lys-Ala-Arg-Val-Nle + 4-nitro-Phe-Glu-Ala-Nle-amide
-
the peptide substrate mimicks the HIV-1 CA/p2 cleavage site
-
-
?
nucleocapsid protein + H2O
?
-
characterization of human immunodeficiency virus type 1 containing mutations in the nucleocapsid protein at a putative HIV-1 protease cleavage site
-
-
?
VLQNYPIVQ + H2O
VLQNY + PIVQ
the protein contains a HIV-1 cleavage site
-
-
?
VVQNYPIVQ + H2O
VVQNY + PIVQ
the protein contains a HIV-1 cleavage site
-
-
?
elF4GI + H2O
additional information
-
-
purified enzyme cleaves at positions 678-679, 681-682 and 1086-1087, separating the three domains of the initiation factor
-
-
?
additional information
?
-
-
insertion of human immunodeficiency virus type 1 protease substrate sequences into the permissive sites converts thymidylate synthase to an HIV-1 protease substrate
-
-
?
additional information
?
-
-
replacement of the P1 amino acid of human immunodeficiency virus type 1 Gag processing sites can inhibit or enhance the rate of cleavage by the viral protease
-
-
?
additional information
?
-
-
autocatalytic maturation, two temporally regulated N-terminal cleavages, first at the native TFP/p6pol followed by cleavage at the p6pol/PR, are crucial for protease maturation and enzymatic activity
-
-
?
additional information
?
-
-
the enzyme exhibits autoprocessing
-
-
?
additional information
?
-
-
artificial neural network method for predicting HIV protease cleavage sites in protein
-
-
?
additional information
?
-
-
sequences surrounding HIV-1 protease cleavage sites in several viral and nonviral protein substrates. No amino acid is required at any of the eight positions of the substrate. The highest preference is seen for glutamate at P2' followed by Phe at P1
-
-
?
additional information
?
-
-
the cleavage site involves a Phe or Tyr as the N-terminal P1 side and a Pro as the C-terminal P1' side of the scissile bond
-
-
?
additional information
?
-
-
the minimum length of effective HIV-1 protease substrate is seven amino acid residues
-
-
?
additional information
?
-
-
autoprocessing of the mature protease from the precursor can either occur in two steps at pH values of 4 to 6 or in a single step above pH 6
-
-
?
additional information
?
-
-
the enzyme plays an essential role in the late-stage maturation step of the virus replication cycle. HIV-1 proteinase autocatalyzes its own cleavage from the Pr165 polyprotein precursor and then cleaves both polyproteins at other specific sites to produce mature proteins
-
-
?
additional information
?
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regulation of the protease in the viral life cycle: transframe region flanking the N-terminus of the protease may function as a negative regulator for protein folding and dimerization. The low dimer stability of the protease precursor relative to that of the mature enzyme is an ideal way of preventing the emergence of enzymatic functions until assembly of the viral particle is complete
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the enzyme is responsible for the processing of gag and gag-pol polyprotein precursors to produce structural proteins and enzymes for the mature virus
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the enzyme facilitates viral maturation by cleaving ten asymmetric and nonhomologous sequences in the Gag and Pol polyproteins
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the enzyme is essential for the replication of the virus
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the enzyme is involved in regulation of the incorporation of reverse transcriptase in the viral early assembly complex comprising reverse transcriptase, genomic RNA, Gag, Gag-Pol, tRNALys, and lysyl tRNA synthetase, HIV-1 protease activity is negatively regulated by the lysyl tRNA synthetase
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amino acid preferences for the critical P2' substrate binding subsite in type 1 cleavage sites, molecular modeling and phylogenetic comparison, overview
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molecular basis for substrate recognition and drug resistance
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substrate and cleavage site sequence specificity, overview, drug resistance occasionally confers a change in substrate specificity, prediction of substrate specificity by three-dimensional structure analysis, detailed overview
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substrate specificity and kinetics of wild-type and mutant enzymes, overview
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comparison of protease specificities for P1, P3, P4 cleaving positions of proteases of HIV-1, HIV-2, equine infectious anemia virus, avian myeloblastosis virus, Mason-Pfizer monkey virus, mouse mammary tumor virus, Moloney murine leukemia virus, human T-lymphotropic virus type 1, bovine leukemia virus, walleye dermal sarcoma virus, and human foamy virus. The retroviral proteases have similar preferences for Phe and Tyr for the P1 position in this sequence context. The sizes of the P3 and P4 residues appear to be a major contributor for specificity
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Arg-Val-Leu-Ala-Glu-Ala-Met mimics the real substrate
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the enzyme prefers to have large hydrophobic amino acids flanking the scissile bond. When P1' is proline, the P2 side chain interacts with a polar region in the S2 subsite of the enzyme, while the P2' amino acid interacts with a hydrophobic region of the S2' subsite. When P1' is not proline, the orientations of the P2 and P2' side chains with respect to the scissile bond are reversed. P2 residues interact with a hydrophobic face of the S2 subsite, while the P2' amino acid usually engages hydrophilic amino acids in the S2' subsite
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