Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.3.6 extracted from

  • Lopez-Villamizar, I.; Cabezas, A.; Pinto, R.; Canales, J.; Ribeiro, J.; Cameselle, J.; Costas, M.
    The characterization of Escherichia coli CpdB as a recombinant protein reveals that, besides having the expected 3'-nucleotidase and 2,3-cyclic mononucleotide phosphodiesterase activities, it is also active as cyclic dinucleotide phosphodiesterase (2016), PLoS ONE, 11, e0148508 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.6

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 and JM109 cells Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.014
-
 3'-AMP at pH 7.5 and 37°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ the enzyme activity is enhanced by 2 mM Co2+ Escherichia coli
Co2+ the enzyme activity is strongly enhanced by 2 mM Co2+ Escherichia coli
Mn2+ 2 mM used in assay conditions Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P08331
-
-

Purification (Commentary)

Purification (Comment) Organism
glutathione-Sepharose column chromatography, Q-Sepharose column chromatography and Sephadex G-100 gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3'-AMP + H2O highly efficient substrate Escherichia coli adenosine + phosphate
-
 ?
additional information the bifunctional enzyme with 3'-nucleotidase and cyclic diadenylate phosphodiesterase activities also exhibits very high efficiencies for 2 ',3 '-cyclic mononucleotides, c-di-GMP, c-di-AMP, 2',3'-cAMP and bis-4-nitrophenylphosphate Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
? x * 69000, fusion protein with glutathione S-transferase, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
3'-NT
-
 Escherichia coli
CpdB the protein has 3 '-nucleotidase and 2 ',3 '-cyclic-mononucleotide phosphodiesterase activities Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
176
-
 3'-AMP at pH 7.5 and 37°C Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
13000
-
 3'-AMP at pH 7.5 and 37°C Escherichia coli