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Literature summary extracted from

  • Abdel Motaal, A.; Tews, I.; Schultz, J.E.; Linder, J.U.
    Fatty acid regulation of adenylyl cyclase Rv2212 from Mycobacterium tuberculosis H37Rv (2006), FEBS J., 273, 4219-4228.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.6.1.1 arachidonic acid strong activation at 0.1 mM Mycobacterium tuberculosis
4.6.1.1 Brij 35
-
 Mycobacterium tuberculosis
4.6.1.1 linoleic acid strong activation at 0.1 mM Mycobacterium tuberculosis
4.6.1.1 linolenic acid strong activation at 0.1 mM Mycobacterium tuberculosis
4.6.1.1 additional information unsaturated fatty acids strongly stimulate Rv2212 activity by increasing substrate affinity, greatly enhance the pH sensitivity, thus converting Rv2212 to a pH sensor adenylyl cyclasemore. At 1 mM, D-galactose, D-mannose, L-arabinose, L-rhamnose, D-glucose, D-fructose, fructose 1,6-bisphosphate, glucose 6-phosphate, DL-threonine, L-isoleucine, L-valine, L-asparagine, L-histidine, L-aspartic acid, D-alanine, L-alanine, L-cysteine, L-leucine, glycine, sodium chloride, potassium chloride, sodium citrate, sodium acetate, sodium bicarbonate, NADH, glyoxylic acid, alpha-ketoglutarate, pyruvate and phosphoenolpyruvate do not significantly affect activity of the holoenzyme Mycobacterium tuberculosis
4.6.1.1 oleic acid strong activation at 0.1 mM Mycobacterium tuberculosis
4.6.1.1 palmitic acid stimulates 3fold Mycobacterium tuberculosis
4.6.1.1 polidocanol
-
 Mycobacterium tuberculosis
4.6.1.1 Triton X-100
-
 Mycobacterium tuberculosis

Application

EC Number Application Comment Organism
4.6.1.1 additional information Rv2212 gene has a domain composition identical to that of the AC isoform Rv1264, limited similarity of the N-termini, N-terminal domain of Rv2212 is not autoinhibitory as in Rv1264 Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.6.1.1 catalytic domain and the holoenzyme expressed in Escherichia coli BL21(DE3)[pREP4] as soluble proteins Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.6.1.1 additional information at 1 mM, D-galactose, D-mannose, L-arabinose, L-rhamnose, D-glucose, D-fructose, fructose 1,6-bisphosphate, glucose 6-phosphate, DL-threonine, L-isoleucine, L-valine, L-asparagine, L-histidine, L-aspartic acid, D-alanine, L-alanine, L-cysteine, L-leucine, glycine, sodium chloride, potassium chloride, sodium citrate, sodium acetate, sodium bicarbonate, NADH, glyoxylic acid, alpha-ketoglutarate, pyruvate and phosphoenolpyruvate do not significantly affect activity of the holoenzyme Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.6.1.1 Mn2+ dependent on Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.1 Mycobacterium tuberculosis P71914 putative adenylate cyclase; H37Rv
-
4.6.1.1 Mycobacterium tuberculosis H37Rv P71914 putative adenylate cyclase; H37Rv
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.6.1.1 catalytic domain and the holoenzyme purified to homogeneity by Ni2+ affinity chromatography Mycobacterium tuberculosis

Storage Stability

EC Number Storage Stability Organism
4.6.1.1 -20°C, 150 mM imidazole, and 2 mM MgCl2, 20% glycerol Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.6.1.1 ATP ATP substrate affinity is low Mycobacterium tuberculosis 3',5'-cAMP + diphosphate
-
 ?
4.6.1.1 ATP ATP substrate affinity is low Mycobacterium tuberculosis H37Rv 3',5'-cAMP + diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
4.6.1.1 dimer gel filtration Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
4.6.1.1 Rv2212
-
 Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.6.1.1 6.5
-
 catalytic domain and the holoenzyme Mycobacterium tuberculosis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.6.1.1 6.5 9 holoenzyme has a 5fold higher activity at pH 6.5 compared to activity at pH 9, and with the catalytic domain the maximal activity difference in activity is 3fold between pH 6.5 and 7.6 Mycobacterium tuberculosis