EC Number |
Inhibitors |
Structure |
---|
4.6.1.18 | 2',3'-dideoxy-3'-glycylamino thymidine |
- |
|
4.6.1.18 | 2',3'-dideoxy-3'-L-alanylamino thymidine |
- |
|
4.6.1.18 | 2',3'-dideoxy-3'-L-histidinylamino thymidine |
- |
|
4.6.1.18 | 2',3'-dideoxy-3'-L-leucylamino thymidine |
- |
|
4.6.1.18 | 2',3'-dideoxy-3'-L-serinylamino thymidine |
occupies the active site of ribonuclease A and preferential perturbs the pKa value of His-119 by its free amino group as found from 1H NMR studies, compounds with polar amino acid side chains such as Ser-aT, Tyr-aT and Trp-aT (except His-aT) are more efficient inhibitors compared to those having hydrophobic side chains |
|
4.6.1.18 | 2',3'-dideoxy-3'-L-tryptophanylamino thymidine |
compounds with polar amino acid side chains such as Ser-aT, Tyr-aT and Trp-aT (except His-aT) are more efficient inhibitors compared to those having hydrophobic side chains |
|
4.6.1.18 | 2',3'-dideoxy-3'-L-tyrosylamino thymidine |
compounds with polar amino acid side chains such as Ser-aT, Tyr-aT and Trp-aT (except His-aT) are more efficient inhibitors compared to those having hydrophobic side chains |
|
4.6.1.18 | 2',3'-dideoxy-3'-L-valinylamino thymidine |
- |
|
4.6.1.18 | 2'-Deoxynucleotides |
- |
|
4.6.1.18 | 3'-CMP |
strong binding by the wild-type enzyme, reduced binding by enzyme mutants T17A and T82A, kinetics, overview |
|