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Literature summary for 4.6.1.1 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
Search for more literature for 4.6.1.1

Activating Compound

Activating Compound Comment Organism Structure
arachidonic acid strong activation at 0.1 mM Mycobacterium tuberculosis
Brij 35
-
 Mycobacterium tuberculosis
linoleic acid strong activation at 0.1 mM Mycobacterium tuberculosis
linolenic acid strong activation at 0.1 mM Mycobacterium tuberculosis
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
oleic acid strong activation at 0.1 mM Mycobacterium tuberculosis
palmitic acid stimulates 3fold Mycobacterium tuberculosis
polidocanol
-
 Mycobacterium tuberculosis
Triton X-100
-
 Mycobacterium tuberculosis

Application

Application Comment Organism
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)

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

Inhibitors

Inhibitors Comment Organism Structure
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

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

Organism

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

Purification (Commentary)

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

Storage Stability

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer gel filtration Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
Rv2212
-
 Mycobacterium tuberculosis

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
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