BRENDA - Enzyme Database show

Fatty acid regulation of adenylyl cyclase Rv2212 from Mycobacterium tuberculosis H37Rv

Abdel Motaal, A.; Tews, I.; Schultz, J.E.; Linder, J.U.; FEBS J. 273, 4219-4228 (2006)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
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
Commentary
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
Commentary
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
Commentary
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
Commentary
Organism
Structure
4.6.1.1
Mn2+
dependent on
Mycobacterium tuberculosis
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
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
Commentary
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.6.1.1
ATP
ATP substrate affinity is low
679750
Mycobacterium tuberculosis
3',5'-cAMP + diphosphate
-
-
-
?
4.6.1.1
ATP
ATP substrate affinity is low
679750
Mycobacterium tuberculosis H37Rv
3',5'-cAMP + diphosphate
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
4.6.1.1
dimer
gel filtration
Mycobacterium tuberculosis
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.6.1.1
6.5
-
catalytic domain and the holoenzyme
Mycobacterium tuberculosis
pH Range
EC Number
pH Minimum
pH Maximum
Commentary
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
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
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 (protein specific)
EC Number
Application
Commentary
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) (protein specific)
EC Number
Commentary
Organism
4.6.1.1
catalytic domain and the holoenzyme expressed in Escherichia coli BL21(DE3)[pREP4] as soluble proteins
Mycobacterium tuberculosis
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
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 (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
4.6.1.1
Mn2+
dependent on
Mycobacterium tuberculosis
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
4.6.1.1
catalytic domain and the holoenzyme purified to homogeneity by Ni2+ affinity chromatography
Mycobacterium tuberculosis
Storage Stability (protein specific)
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) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.6.1.1
ATP
ATP substrate affinity is low
679750
Mycobacterium tuberculosis
3',5'-cAMP + diphosphate
-
-
-
?
4.6.1.1
ATP
ATP substrate affinity is low
679750
Mycobacterium tuberculosis H37Rv
3',5'-cAMP + diphosphate
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
4.6.1.1
dimer
gel filtration
Mycobacterium tuberculosis
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.6.1.1
6.5
-
catalytic domain and the holoenzyme
Mycobacterium tuberculosis
pH Range (protein specific)
EC Number
pH Minimum
pH Maximum
Commentary
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