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Information on EC 3.4.23.16 - HIV-1 retropepsin

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.16 HIV-1 retropepsin
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UNIPROT: Q7SSI0 not found.
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro
Synonyms
hiv-1 protease, hiv protease, hiv-1 pr, hiv pr, human immunodeficiency virus protease, hiv-1 proteinase, human immunodeficiency virus type 1 protease, gag protease, hivpr, hiv-1pr, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Gag protease
-
-
-
-
HIV aspartyl protease
-
-
-
-
HIV-1 protease
-
-
-
-
HIV-1 proteinase
-
-
-
-
human immunodeficiency virus type 1 protease
-
-
-
-
retropepsin
-
-
-
-
retroproteinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
144114-21-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
AETFYVDG + H2O
AETF + YVDG
show the reaction diagram
-
-
-
?
ARVLAEAM + H2O
ARVL + AEAM
show the reaction diagram
-
-
-
?
ATIMMQRG + H2O
ATIM + MQRG
show the reaction diagram
-
-
-
?
DCAWLEAQ + H2O
DCAW + LEAQ
show the reaction diagram
-
-
-
?
Gag polyprotein + H2O
?
show the reaction diagram
Gag-Pol polyprotein + H2O
?
show the reaction diagram
-
-
-
?
NLAFPQGE + H2O
NLAF + PQG
show the reaction diagram
-
-
-
?
PGNFLQSR + H2O
PGNF + LQSR
show the reaction diagram
-
-
-
?
RKVLFLDG + H2O
RKVL + FLDG
show the reaction diagram
-
-
-
?
RQANFLGK + H2O
RQAN + FLGK
show the reaction diagram
-
-
-
?
RQANFLRE + H2O
RQAN + FLRE
show the reaction diagram
-
-
-
?
SQNYPIVQ + H2O
SQNY + PIVQ
show the reaction diagram
-
-
-
?
TLNFPISP + H2O
TLNF + PISP
show the reaction diagram
-
-
-
?
TLNFPQIT + H2O
TLNF + PQIT
show the reaction diagram
-
-
-
?
TNIMMQKS + H2O
TNIM + MQKS
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Gag polyprotein + H2O
?
show the reaction diagram
Gag-Pol polyprotein + H2O
?
show the reaction diagram
-
-
-
?
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000039 - 0.0000035
amprenavir
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is essential to the replication and invasion of HIV and is responsible for cleaving large polyprotein precursors Gag and releasing small structural proteins to help the assembly of infectious viral particles
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q7SSI0_9HIV1
99
0
10777
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.25 M sodium citrate pH 6.0, 10% (v/v) DMSO, and 40%-60% (w/v) saturated ammonium sulfate
mutant enzyme V32I/I47V/V82I in complex with amprenavir, sitting drop vapor diffusion method, using 0.1M MES, 0.9 M NaCl, pH 6.0 in H2O
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D29N
the mutation can largely reduce the binding capability of the two peptides ARVLAEAM and NLAFPQGE as compared to the wild type enzyme
I54V
the mutant enzyme is resistant against inhibition by darunavir and nelfinavir
L10I
the mutant enzyme is resistant against inhibition by darunavir and tipranavir
L10I/G48V/I54V/V82A
multi-drug-resistant variant
L90M
the mutant enzyme is resistant against inhibition by darunavir and tipranavir
M46L
the mutant enzyme is resistant against inhibition by darunavir and saquinavir
N25D
the mutation completely eliminates the binding capability of the two peptides ARVLAEAM and NLAFPQGE as compared to the wild type enzyme
V32I/I47V/V82I
the three mutations do not significantly alter the interaction between inhibitor amprenavir and the enzyme
V82T
the mutant enzyme is resistant against inhibition by darunavir
V82T/I84V
multi-drug-resistant variant
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
high performance liquid chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21-Gold (DE3)pLysS cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gerlits, O.; Keen, D.A.; Blakeley, M.P.; Louis, J.M.; Weber, I.T.; Kovalevsky, A.
Room temperature neutron crystallography of drug resistant HIV-1 protease uncovers limitations of X-ray structural analysis at 100 K
J. Med. Chem.
60
2018-2025
2017
Human immunodeficiency virus 1 (Q7SSI0), Human immunodeficiency virus 1
Manually annotated by BRENDA team
Lv, Y.; Li, J.; Fang, J.; Jiao, X.; Yan, L.; Shan, B.
Systematic profiling of substrate binding response to multidrug-resistant mutations in HIV-1 protease Implication for combating drug resistance
J. Mol. Graph. Model.
74
83-88
2017
Human immunodeficiency virus 1 (Q7SSI0), Human immunodeficiency virus 1
Manually annotated by BRENDA team
Olajuyigbe, F.M.; Demitri, N.; De Zorzi, R.; Geremia, S.
Developing HIV-1 protease inhibitors through stereospecific reactions in protein crystals
Molecules
21
1458
2016
Human immunodeficiency virus 1 (Q7SSI0), Human immunodeficiency virus 1
Manually annotated by BRENDA team
Yu, Y.; Wang, J.; Shao, Q.; Shi, J.; Zhu, W.
Effects of drug-resistant mutations on the dynamic properties of HIV-1 protease and inhibition by amprenavir and darunavir
Sci. Rep.
5
10517
2015
Human immunodeficiency virus 1 (Q7SSI0), Human immunodeficiency virus 1
Manually annotated by BRENDA team