EC Number | Crystallization (Comment) | Organism |
---|---|---|
4.6.1.1 | 3.3 A resolution active form of the catalytic domain Rv1264, 2.3 A resolution inhibited form | Mycobacterium tuberculosis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.6.1.1 | E195A | mutation with partially relieved inhibition and 4fold increased enzyme activity at pH 8.0, pH optimum shifted from 5.8 to 6.5 | Mycobacterium tuberculosis |
4.6.1.1 | H192A | mutant with wild-type phenotype at pH 8.0, the slope of activation is shifted by 0.5 pH units towards the acidic pH. 10fold higher enzyme activity at pH 8.0 than the wild type | Mycobacterium tuberculosis |
4.6.1.1 | R309A | mutation renders holoenzyme active and unregulated | Mycobacterium tuberculosis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.6.1.1 | Mycobacterium tuberculosis | P9WQ35 | - |
- |
4.6.1.1 | Mycobacterium tuberculosis H37Rv | P9WQ35 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.6.1.1 | - |
Mycobacterium tuberculosis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.6.1.1 | ATP | - |
Mycobacterium tuberculosis | cAMP + diphosphate | - |
? | |
4.6.1.1 | ATP | - |
Mycobacterium tuberculosis H37Rv | cAMP + diphosphate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.6.1.1 | adenylyl cyclase | - |
Mycobacterium tuberculosis |
4.6.1.1 | Rv1264 | - |
Mycobacterium tuberculosis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.6.1.1 | 5.8 | - |
holoenzyme | Mycobacterium tuberculosis |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
4.6.1.1 | 4.8 | 8 | holoenzyme | Mycobacterium tuberculosis |
4.6.1.1 | 5.5 | 8 | isolated catalytic domain Rv1264 211-397, uniformly high enzyme activity | Mycobacterium tuberculosis |