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Literature summary extracted from

  • Tews, I.; Findeisen, F.; Sinning, I.; Schultz, A.; Schultz, J.E.; Linder, J.U.
    The Structure of a pH-Sensing Mycobacterial Adenylyl Cyclase Holoenzyme (2005), Science, 308, 1020-1023.
    View publication on PubMed

Crystallization (Commentary)

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

Protein Variants

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

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
-
Mycobacterium tuberculosis

Substrates and Products (Substrate)

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
-
?

Synonyms

EC Number Synonyms Comment Organism
4.6.1.1 adenylyl cyclase
-
Mycobacterium tuberculosis
4.6.1.1 Rv1264
-
Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.6.1.1 5.8
-
holoenzyme Mycobacterium tuberculosis

pH Range

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