EC Number   |
Protein Variants |
Reference |
|---|
   3.4.23.B3 | I54G |
mutant enzyme is only marginally different from wild-type enzyme in its susceptibility to most of the inhibitors of the HIV-1/HIV-2 proteinases. LP-149 shows a ninefold reduction in potency against the mutant enzyme. Pro-Ser-Glu-Glu-Tyr-Pro-Ile-2-aminohexanoic acid-Ile-Asn is cleaved less efficiently than by the wild-type enzyme. The ability to hydrolyze Gln-Lys-2-aminohexanoic acid-2-aminohexanoic acid-Leu-p-nitrophenylalanine-Ala-Lys-Ala-Leu is lowered by at least 100fold compared to wild-type enzyme |
647821 |
| 3.4.23.B3 | I54G |
the ability of the mutant enzyme to cleave the pseudosymmetrical peptide substrate Ac-Tyr-Arg-Ala-Arg-Val-Phe-4-nitrophenylalanyl-Val-Arg-Ala-Ala-Lys is more than an order of magnitude lower than that of the wild-type enzyme |
647825 |
| 3.4.23.B3 | I54G/Y48H |
specificity constant is only 3fold lower than that measured for the single mutant I54G enzyme, towards the long, pseudosymmetrical peptide substrate Ac-Tyr-Arg-Ala-Arg-Val-Phe-4-nitrophenylalanyl-Val-Arg-Ala-Ala-Lys. The potency of the shorter HBY-793 inhibitor is reduced by 60fold compared to the Ki values measured against the wild-type or the I54G mutant enzyme |
647825 |
| 3.4.23.B3 | T30D |
mutant enzyme is only marginally different from wild-type enzyme in its susceptibility to most of the inhibitors of the HIV-1/HIV-2 proteinases, except that HBY-793 has a potency that is reduced by ten-fold |
647821 |
