EC Number   |
General Information |
Reference |
|---|
   3.4.23.B8 | malfunction |
hydrophobic force plays an important role in suppressing protease activity especially for HTLV-1 protease, which in turn prevents the virus maturity |
754685 |
| 3.4.23.B8 | more |
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 |
754687 |
| 3.4.23.B8 | more |
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 |
754685 |
| 3.4.23.B8 | physiological function |
HTLV-1 protease is an aspartic protease and crucial for processing of the virus proteins |
711453 |
| 3.4.23.B8 | physiological function |
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 |
754685 |
| 3.4.23.B8 | physiological function |
the enzyme is required in the virus replication mechanism |
754687 |
