3.4.23.B8: human T-cell leukemia virus type 1 protease
This is an abbreviated version!
For detailed information about human T-cell leukemia virus type 1 protease, go to the full flat file.
Word Map on EC 3.4.23.B8
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3.4.23.B8
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retroviral
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polyproteins
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spastic
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retroviruses
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myelopathy
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tetrapeptidic
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paraparesis
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indinavir
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hydroxyethylamine
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aspartyl
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substrate-based
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scissile
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peptidomimetic
-
medicine
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hydroxymethylcarbonyl
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autoprocessing
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darunavir
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gag-pro-pol
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drug development
- 3.4.23.B8
-
retroviral
- polyproteins
-
spastic
-
retroviruses
- myelopathy
-
tetrapeptidic
- paraparesis
- indinavir
-
hydroxyethylamine
-
aspartyl
-
substrate-based
-
scissile
-
peptidomimetic
- medicine
-
hydroxymethylcarbonyl
-
autoprocessing
- darunavir
-
gag-pro-pol
- drug development
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
C2A HTLV-1 PR, HTLV-1 PR, HTLV-1 protease, HTLV-I PR, HTLV-I protease, human T cell leukemia virus PR, human T cell leukemia virus protease, human T-cell leukemia virus type 1 protease, human T-lymphotropic virus type I protease, More, retropepsin (human T-cell leukemia virus), simian T-cell leukemia virus endopeptidase
ECTree
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General Information
General Information on EC 3.4.23.B8 - human T-cell leukemia virus type 1 protease
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malfunction
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hydrophobic force plays an important role in suppressing protease activity especially for HTLV-1 protease, which in turn prevents the virus maturity
physiological function
additional information
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HTLV-1 protease is an aspartic protease and crucial for processing of the virus proteins
physiological function
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HTLV-1 protease is an aspartic protease responsible for the processing of Gag and Gag-pro-pol polyprotein during virus maturation and catalyzes an essential step in virus replication cycle
physiological function
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the enzyme is required in the virus replication mechanism
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the active sites are located between the two monomer chains comprising residues Arg10, Leu30, Asp32, Gly34, Ala35, Asp36, Met37, Val39, Leu56, Leu57, Ala59, Leu91, Trp98, and Ile100
additional information
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two acidic residues are located in the narrow tunnel-shaped active site of enzyme accommodating substrates or inhibitors. The residues located in the HTLV-1 active site include Arg10, Lys95, Asn96, and Asn97 in the S3 subsite, residues Asp36, Met37, Asn53, Thr54, Ser55, Cys90, and Val92 in the S4 subsite, and residues Leu30, Gly34, Val56, Leu57, Gln96, Gln97, Trp98 in the S1 subsite, as well as two catalytic aspartyl residues (Asp32) positioned in both symmetrical chains of protease