EC Number   |
Protein Variants |
Reference  |
|---|
   6.2.1.45 | D576A |
Km-value for ATP is 37.8fold higher than wild-type value, KM-value for ubiquitin is 36fold higher than wild-type value. kcat for ubiquitin adenylate formation is 250fold lower than wild-type value. kcat for ubiquitin carrier protein E2 transthiolation is 28.3fold lower than wild-type value |
674561 |
| 6.2.1.45 | D576A |
mutation within the MgATP2- binding site, results in dramatically impaired binding affinities for MgATP2-, a shift from ordered to random addition in co-substrate binding, and a significantly reduced rate of ternary complex formation that shifts the rate-limiting step to ubiquitin adenylate formation. Mutations does not affect the affinity of Ubc2b binding, however, differences in kcat values determined from ternary complex formation versus HsUbc2b transthiolation suggest that binding of the E2 enhances the rate of bound ubiquitin adenylate formation |
674561 |
| 6.2.1.45 | D576E |
Km-value for ATP is 4fold higher than wild-type value, KM-value for ubiquitin is 1.4fold higher than wild-type value. kcat for ubiquitin adenylate formation is 1200fold lower than wild-type value. kcat for ubiquitin carrier protein E2 transthiolation is 34fold lower than wild-type value |
674561 |
| 6.2.1.45 | D576E |
mutation within the MgATP2- binding site, results in dramatically impaired binding affinities for MgATP2-, a shift from ordered to random addition in co-substrate binding, and a significantly reduced rate of ternary complex formation that shifts the rate-limiting step to ubiquitin adenylate formation. Mutations does not affect the affinity of Ubc2b binding, however, differences in kcat values determined from ternary complex formation versus HsUbc2b transthiolation suggest that binding of the E2 enhances the rate of bound ubiquitin adenylate formation |
674561 |
| 6.2.1.45 | D576N |
Km-value for ATP is 5.2fold higher than wild-type value, KM-value for ubiquitin is 5fold higher than wild-type value. kcat for ubiquitin adenylate formation is 545fold lower than wild-type value. kcat for ubiquitin carrier protein E2 transthiolation is 155fold lower than wild-type value |
674561 |
| 6.2.1.45 | D576N |
mutation within the MgATP2- binding site, results in dramatically impaired binding affinities for MgATP2-, a shift from ordered to random addition in co-substrate binding, and a significantly reduced rate of ternary complex formation that shifts the rate-limiting step to ubiquitin adenylate formation. Mutations does not affect the affinity of Ubc2b binding, however, differences in kcat values determined from ternary complex formation versus HsUbc2b transthiolation suggest that binding of the E2 enhances the rate of bound ubiquitin adenylate formation |
674561 |
| 6.2.1.45 | K528A |
Km-value for ATP is 1.6fold higher than wild-type value, KM-value for ubiquitin is 2.9fold higher than wild-type value. kcat for ubiquitin adenylate formation is 400fold lower than wild-type value. kcat for ubiquitin carrier protein E2 transthiolation is 309fold lower than wild-type value |
674561 |
| 6.2.1.45 | K528A |
mutation within the MgATP2- binding site, results in dramatically impaired binding affinities for MgATP2-, a shift from ordered to random addition in co-substrate binding, and a significantly reduced rate of ternary complex formation that shifts the rate-limiting step to ubiquitin adenylate formation. Mutations does not affect the affinity of Ubc2b binding, however, differences in kcat values determined from ternary complex formation versus HsUbc2b transthiolation suggest that binding of the E2 enhances the rate of bound ubiquitin adenylate formation |
674561 |
| 6.2.1.45 | more |
only full-length GSTHsUba1a is catalytically active |
674561 |
| 6.2.1.45 | more |
a mutational reduction in Uba1 function (Uba1B2 mutation) reduces the efficacy of cell death, a complete loss of Uba1 function (Uba1A1 mutation) results in poor survival of mutant tissue and overgrowth of adjacent wild type tissue |
692413 |
