EC Number   |
Protein Variants |
Reference |
|---|
  2.8.1.B2 | C225A |
the Uba4-C225A variant has a slower rate of molybdopterin production in Escherichia coli in comparison to that of wild-type Uba4 likely due to the reduced stability of the protein |
690968 |
| 2.8.1.B2 | C225A/C397A |
comparison of the efficiencies of Uba4 and the C397A and C225A/C397A variants in producing molybdopterin in the presence of thiosulfate reveals that residue Cys397 is essential for sulfuration of human MOCS2A. Thus, the resulting persulfide group on Cys397 of Uba4 is specifically transferred to MOCS2A during the reaction |
690968 |
| 2.8.1.B2 | C225A/C397A |
slightly different amounts of molybdopterin produced by the Uba4 variant C225A/C397A in Escherichia coli are likely due to the reduced stability of the protein |
690968 |
| 2.8.1.B2 | C225S |
when a plasmid harboring UBA4 with a C225S mutation is introduced into the DELTAUBA4 strain, no thiouridine formation of tRNAGlu can be observed, demonstrating that Cys225 is the active-site cysteine residue of UBA4 required for 2-thiouridine formation |
694464 |
| 2.8.1.B2 | C397A |
comparison of the efficiencies of Uba4 and the C397A and C225A/C397A variants in producing molybdopterin in the presence of thiosulfate reveals that residue Cys397 is essential for sulfuration of human MOCS2A. Thus, the resulting persulfide group on Cys397 of Uba4 is specifically transferred to MOCS2A during the reaction |
690968 |
| 2.8.1.B2 | C397S |
approximately half the fraction of tRNAGlu in the DELTAUBA4 strain can be 2-thiolated by the introduction of a plasmid encoding the wild-type UBA4. When pUBA4 C397S is introduced, no 2-thiouridine formation of tRNAGlu occurrs. Cys397 in the rhodanese-like domain (RLD) of UBA4 is critical for 2-thiouridine formation |
694464 |
