Literature summary for 2.7.7.85 extracted from

Rosenberg, J.; Dickmanns, A.; Neumann, P.; Gunka, K.; Arens, J.; Kaever, V.; Stuelke, J.; Ficner, R.; Commichau, F.M.
Structural and biochemical analysis of the essential diadenylate cyclase CdaA from Listeria monocytogenes (2015), J. Biol. Chem., 290, 6596-6606.

Search for more literature for 2.7.7.85

Cloned(Commentary)

Cloned (Comment)	Organism
expression of truncated CdaA variants in Escherichia coli	Listeria monocytogenes

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of N-terminally truncated protein lacking first 100 residues, i.e. the transmembrane domain and the CC motif, to 2.8 A resolution. The protein exhibits an overall globular fold with the long N-terminally located helix (alpha1) flanking the core	Listeria monocytogenes

Protein Variants

Protein Variants	Comment	Organism
additional information	both N-terminally truncated protein lacking first 100 residues, i.e. the transmembrane domain and the CC motif, and the N-terminally truncated protein lacking first 80 residues are enzymatically active, The shorter DAC variant is 6.5fold more active than the longer variant	Listeria monocytogenes

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Co2+	or Mn2+, required. Maximum activity at 0.75-10 mM	Listeria monocytogenes
Mn2+	or Co2+, required. Maximum activity at 0.75-5 mM	Listeria monocytogenes

Organism

Organism	UniProt	Comment	Textmining
Listeria monocytogenes	Q8Y5E4	-	-
Listeria monocytogenes ATCC BAA-679	Q8Y5E4	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)