EC Number   |
Protein Variants |
Reference |
|---|
  2.7.7.89 | D173N/D175N |
complete loss of adenylyl-removing activity, while adenylyltransferase activity is retained |
-, 672242 |
| 2.7.7.89 | D463N/P467A/L469G |
mutant enzyme has approximately one-half to one-third of the adenylyl-removing activity observed with the wild-type enzyme, and this adenylyl-removing activity is inhibited by PII and by glutamine like the wild-type enzyme. The mutant enzyme also has approximately one-half to one-third of the adenylyltransferase activity when compared to the wild-type enzyme, and this activity is regulated normally by glutamine, PII, and PII-UMP |
-, 672242 |
| 2.7.7.89 | D701N/D703N |
complete loss of adenylyltransferase activity, while adenylyl-removing activity is retained |
-, 672242 |
| 2.7.7.89 | more |
construcution of truncation mutants corresponding to amino acids 1-423 (AT-N) and 425-945 (AT-C). AT-N carries a deadenylylation activity and AT-C carries an adenylylation activity |
733719 |
| 2.7.7.89 | more |
expression of soluble N-terminal domain, residues 1-440, of the Escherichia coli adenylyl transferase responsible for deadenylylation activity. The domain is truncated at the end of a predicted helix and prior to a Q-linker, it is very soluble and stable. The construct has deadenylylation activity that is independent of the low nitrogen status indicator PII-UMP |
735210 |
| 2.7.7.89 | more |
truncated versions of ATase missing the C-terminal domain lacked both adenylyltransferase and the adenylyl-removing activity, suggesting a role for the C-terminal nucleotidyltransferase domain in both activities. The purified C-terminal nucleotidyltransferase domain and larger polypeptides containing this domain have significant basal AT activity, which is stimulated by glutamine. A truncated enzyme lacking amino acids 456-577 from the central region shows complete loss of adenylyl-removing activity, while adenylyltransferase activity is retained. Mutation converts signal transduction protein PII from an activator to an inhibitor |
-, 672242 |
| 2.7.7.89 | R499A/R501A/D505N/P509A/L511G |
mutant enzyme completely lacks adenylyl-removing activity but retains adenylyltransferase activity. Mutant exhibits significant basal adenylyltransferase activity in the absence of any activators |
-, 672242 |
