Literature summary for 4.6.1.1 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.

Search for more literature for 4.6.1.1

Crystallization (Commentary)

Crystallization (Comment)	Organism
3.3 A resolution active form of the catalytic domain Rv1264, 2.3 A resolution inhibited form	Mycobacterium tuberculosis

Protein Variants

Protein Variants	Comment	Organism
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
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
R309A	mutation renders holoenzyme active and unregulated	Mycobacterium tuberculosis

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	P9WQ35	-	-
Mycobacterium tuberculosis H37Rv	P9WQ35	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP	-	Mycobacterium tuberculosis	cAMP + diphosphate	-	?
ATP	-	Mycobacterium tuberculosis H37Rv	cAMP + diphosphate	-	?

Synonyms

Synonyms	Comment	Organism
adenylyl cyclase	-	Mycobacterium tuberculosis
Rv1264	-	Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5.8	-	holoenzyme	Mycobacterium tuberculosis

pH Range

pH Minimum	pH Maximum	Comment	Organism
4.8	8	holoenzyme	Mycobacterium tuberculosis
5.5	8	isolated catalytic domain Rv1264 211-397, uniformly high enzyme activity	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)