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Literature summary for 3.1.4.17 extracted from

  • Schulte, J.; Baumgart, M.; Bott, M.
    Identification of the cAMP phosphodiesterase CpdA as novel key player in cAMP-dependent regulation in Corynebacterium glutamicum (2017), Mol. Microbiol., 103, 534-552 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Corynebacterium glutamicum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.23
-
3',5'-cGMP apparent value, at pH 7.5 and 30°C Corynebacterium glutamicum
2.54
-
3',5'-cAMP apparent value, at pH 7.5 and 30°C Corynebacterium glutamicum

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ contains 2.8 zinc atoms per molecule of purified enzyme Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3',5'-cAMP + H2O Corynebacterium glutamicum
-
5'-AMP
-
?
3',5'-cAMP + H2O Corynebacterium glutamicum ATCC 13032
-
5'-AMP
-
?

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum
-
-
-
Corynebacterium glutamicum ATCC 13032
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography and Superdex 200 gel filtration Corynebacterium glutamicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3',5'-cAMP + H2O
-
Corynebacterium glutamicum 5'-AMP
-
?
3',5'-cAMP + H2O
-
Corynebacterium glutamicum ATCC 13032 5'-AMP
-
?
3',5'-cGMP + H2O
-
Corynebacterium glutamicum 5'-GMP
-
?
3',5'-cGMP + H2O
-
Corynebacterium glutamicum ATCC 13032 5'-GMP
-
?
bis-(4-nitrophenyl) phosphate + H2O
-
Corynebacterium glutamicum 4-nitrophenyl phosphate + 4-nitrophenol
-
?
bis-(4-nitrophenyl) phosphate + H2O
-
Corynebacterium glutamicum ATCC 13032 4-nitrophenyl phosphate + 4-nitrophenol
-
?
additional information the enzyme is unable to dephosphorylate 5'-AMP Corynebacterium glutamicum ?
-
?
additional information the enzyme is unable to dephosphorylate 5'-AMP Corynebacterium glutamicum ATCC 13032 ?
-
?

Subunits

Subunits Comment Organism
dimer or tetramer gel filtration Corynebacterium glutamicum

Synonyms

Synonyms Comment Organism
cAMP phosphodiesterase
-
Corynebacterium glutamicum
cAMP-PDE
-
Corynebacterium glutamicum
cg2761
-
Corynebacterium glutamicum
CpdA
-
Corynebacterium glutamicum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65 70
-
Corynebacterium glutamicum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
18.1
-
3',5'-cAMP apparent value, at pH 7.5 and 30°C Corynebacterium glutamicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 7
-
Corynebacterium glutamicum

General Information

General Information Comment Organism
malfunction a deletion mutant shows a 2fold increased cAMP level on D-glucose and reduced growth rates on carbon sources Corynebacterium glutamicum
physiological function the enzyme plays a key role in the control of the cellular cAMP concentration and transcriptional regulator GlxR activity and is crucial for optimal metabolism and growth of Corynebacterium glutamicum Corynebacterium glutamicum