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Literature summary extracted from
- The structure of the regulatory domain of the adenylyl cyclase Rv1264 from Mycobacterium tuberculosis with bound oleic acid (2007), J. Mol. Biol., 369, 1282-1295.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.6.1.1 | additional information | regulatory domain of Rv1264 regulates AC activity in a pH-dependent manner, activated at acidic pH due to pH-dependent structural transitions of the Rv1264 dimer, strongly activated by the addition of fatty acids, oleic acid may serve as a hinge | Mycobacterium tuberculosis |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.6.1.1 | overexpression of the histidine-tagged auto-inhibitory domain Rv1264N in Escherichia coli BL21(DE3)[pREP4] cells | Mycobacterium tuberculosis |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.6.1.1 | by the hanging-drop, vapour-diffusion method at 18°C, to 1.6 A resolution, crystal structure of the histidine-tagged auto-inhibitory domain Rv1264N shows the protein in a tight, disk-shaped dimer, formed around a helical bundle, and involving a protein chain crossover | Mycobacterium tuberculosis |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.6.1.1 | E136A | shift of the pH optimum by about 0.5 unit to acidic pH | Mycobacterium tuberculosis |
| 4.6.1.1 | E136R | shift of the pH optimum by about 0.5 unit to acidic pH | Mycobacterium tuberculosis |
| 4.6.1.1 | H103A | pH regulation is barely affected, not involved in pH-regulation | Mycobacterium tuberculosis |
| 4.6.1.1 | H140A | pH regulation is barely affected, not involved in pH-regulation, shift of the pH optimum by about 0.5 unit to acidic pH | Mycobacterium tuberculosis |
| 4.6.1.1 | H140R | inhibition is relaxed slightly, with a shift of the pH optimum toward more basic values | Mycobacterium tuberculosis |
| 4.6.1.1 | H58A | pH regulation is barely affected, not involved in pH-regulation | Mycobacterium tuberculosis |
| 4.6.1.1 | additional information | deletion in the shoulder domain of the holoenzyme, linking of the two adjoining Calpha positions of residues Ala93 and His103, which are 4.6 A apart, mutant enzyme is 7fold more active at pH 8.0 compared to the wild-type enzyme, and shows only a residual 3fold activation at pH 5.5. When the entire shoulder domain is deleted, residues Asp62 to Arg105, the phenotype is similar. This deletion joins the Calpha positions of residues Gly61 and Ala106, which are 6.4 A apart in the wild-type structure | Mycobacterium tuberculosis |
| 4.6.1.1 | R132A | shift of the pH optimum by about 0.5 unit to acidic pH | Mycobacterium tuberculosis |
| 4.6.1.1 | R132E | results in a biphasic pH activity curve with a minimum at pH 6.5 and higher activity at basic pH values | Mycobacterium tuberculosis |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.6.1.1 | additional information | addition of one or two residues results in a slightly more inhibited phenotype. Addition of three residues results in only subtle changes, probably because the insertion of three residues is compatible with an extra-helical turn. In contrast, insertion of nine amino acids almost abolishes pH sensitivity | Mycobacterium tuberculosis |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.6.1.1 | Mn2+ | - |
Mycobacterium tuberculosis |  |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.6.1.1 | 45000 | - |
histidine-tagged auto-inhibitory domain Rv1264N, gel filtration | Mycobacterium tuberculosis |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.6.1.1 | Mycobacterium tuberculosis | P9WQ35 | - |
- |
| 4.6.1.1 | Mycobacterium tuberculosis H37Rv | P9WQ35 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.6.1.1 | histidine-tagged auto-inhibitory domain Rv1264N, on nickel nitrilotriacetic acid/agarose column, to purity | Mycobacterium tuberculosis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.6.1.1 | ATP | - |
Mycobacterium tuberculosis | 3',5'-cAMP + diphosphate | - |
? | |
| 4.6.1.1 | ATP | - |
Mycobacterium tuberculosis H37Rv | 3',5'-cAMP + diphosphate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.6.1.1 | dimer | histidine-tagged auto-inhibitory domain Rv1264N, gel filtration | Mycobacterium tuberculosis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.6.1.1 | class III AC | - |
Mycobacterium tuberculosis |
| 4.6.1.1 | Rv1264 | - |
Mycobacterium tuberculosis |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.6.1.1 | 5 | 8 | - |
Mycobacterium tuberculosis |
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Release 2023.1 (January 2023)
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