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Literature summary extracted from

  • Keppetipola, N.; Shuman, S.
    A phosphate-binding histidine of binuclear metallophosphodiesterase enzymes is a determinant of 2,3-cyclic nucleotide phosphodiesterase activity (2008), J. Biol. Chem., 283, 30942-30949.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.4.16 expressed in Escherichia coli strain BL21(DE3) Mycobacterium tuberculosis
3.1.4.16 expressed in Escherichia coli strain BL21(DE3) Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
3.1.4.16 H98A the mutation suppresses the 2',3'-cAMP phosphodiesterase activity of Rv0805 without adversely affecting hydrolysis of bis-p-nitrophenyl phosphate Mycobacterium tuberculosis
3.1.4.16 H98A the mutation suppresses the 2',3'-cAMP phosphodiesterase activity of Rv0805 without adversely affecting hydrolysis of bis-p-nitrophenyl phosphate Escherichia coli
3.1.4.16 H98D the mutation suppresses the 2',3'-cAMP phosphodiesterase activity of Rv0805 without adversely affecting hydrolysis of bis-p-nitrophenyl phosphate Mycobacterium tuberculosis
3.1.4.16 H98D the mutation suppresses the 2',3'-cAMP phosphodiesterase activity of Rv0805 without adversely affecting hydrolysis of bis-p-nitrophenyl phosphate Escherichia coli
3.1.4.16 H98N the mutation suppresses the 2',3'-cAMP phosphodiesterase specific activity to one-fifth the level of wild type Rv0805 Mycobacterium tuberculosis
3.1.4.16 H98N the mutation suppresses the 2',3'-cAMP phosphodiesterase specific activity to one-fifth the level of wild type Rv0805 Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.4.16 phosphate
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.4.16 0.9
-
 bis-p-nitrophenyl phosphate wild type enzyme, in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2 Mycobacterium tuberculosis
3.1.4.16 1.6
-
 cyclic 2',3'-AMP wild type enzyme, in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2 Mycobacterium tuberculosis
3.1.4.16 1.7
-
 p-nitrophenyl phosphate wild type enzyme, in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2 Mycobacterium tuberculosis
3.1.4.16 6
-
 p-nitrophenyl phosphate in Tris-HCl buffer (pH 8.5) in the presence of 5 mM MnCl2 Escherichia coli
3.1.4.16 9.3
-
 bis-p-nitrophenyl phosphate in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2 Escherichia coli
3.1.4.16 35
-
 cyclic 2',3'-AMP in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.4.16 Mn2+ dependent on Mycobacterium tuberculosis
3.1.4.16 Mn2+ dependent on Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.16 Escherichia coli P67095
-
-
3.1.4.16 Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.4.16 Ni-NTA agarose column chromatography Mycobacterium tuberculosis
3.1.4.16 Ni-NTA agarose column chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.16 bis-p-nitrophenyl phosphate + H2O
-
 Mycobacterium tuberculosis p-nitrophenol + p-nitrophenyl phosphate
-
 ?
3.1.4.16 bis-p-nitrophenyl phosphate + H2O
-
 Escherichia coli p-nitrophenol + p-nitrophenyl phosphate
-
 ?
3.1.4.16 cyclic 2',3'-AMP + H2O Rv0805 is 150fold more active in hydrolyzing 2',3'-cAMP than 3',5'-cAMP, the enzyme hydrolyzes either P-O2' or P-O3' bonds to yield a mixture of 3'-AMP and 2'-AMP products, with a bias toward 3'-AMP Mycobacterium tuberculosis 3'-AMP
-
 ?
3.1.4.16 cyclic 2',3'-AMP + H2O YfcE-C74H cleaves exclusively the P-O2' bond of 2',3'-cAMP Escherichia coli 3'-AMP
-
 ?
3.1.4.16 cyclic 2',3'-GMP + H2O
-
 Mycobacterium tuberculosis 3'-GMP
-
 ?
3.1.4.16 cyclic 2',3'-GMP + H2O
-
 Escherichia coli 3'-GMP
-
 ?
3.1.4.16 cyclic 3',5'-AMP + H2O weak activity Escherichia coli 5'-AMP
-
 ?
3.1.4.16 cyclic 3',5'-AMP + H2O weak activity, Rv0805 is 150fold more active in hydrolyzing 2',3'-cAMP than 3',5'-cAMP Mycobacterium tuberculosis 5'-AMP
-
 ?
3.1.4.16 cyclic 3',5'-GMP + H2O weak activity Mycobacterium tuberculosis 5'-GMP
-
 ?
3.1.4.16 cyclic 3',5'-GMP + H2O weak activity Escherichia coli 5'-GMP
-
 ?
3.1.4.16 cyclic 3',5'-UMP + H2O weak activity Mycobacterium tuberculosis 5'-UMP
-
 ?
3.1.4.16 cyclic 3',5'-UMP + H2O weak activity Escherichia coli 5'-UMP
-
 ?
3.1.4.16 additional information the enzyme does not have a preference for 2',3'-cAMP versus 2',3'-cGMP Mycobacterium tuberculosis ?
-
 ?
3.1.4.16 additional information YfcE-C74H has no detectable ability to hydrolyze phosphomonoester substrates 5'-AMP, 3'-AMP, or 2'-AMP Escherichia coli ?
-
 ?
3.1.4.16 p-nitrophenyl phosphate + H2O
-
 Escherichia coli p-nitrophenol + phosphate
-
 ?
3.1.4.16 p-nitrophenyl phosphate + H2O weak activity Mycobacterium tuberculosis p-nitrophenol + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.4.16 2,3-cyclic nucleotide phosphodiesterase
-
 Mycobacterium tuberculosis
3.1.4.16 Rv0805 functions as a 3',5'-cyclic nucleotide phosphodiesterase but has also 2',3'-cyclic nucleotide phosphodiesterase function Mycobacterium tuberculosis
3.1.4.16 YfcE-C74H the mutant enzyme is strictly specific for 2',3'-cNMP, the C74H mutation uniquely confers a gain of function in hydrolysis of 2',3'-cAMP Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.4.16 0.55
-
 p-nitrophenyl phosphate wild type enzyme, in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2 Mycobacterium tuberculosis
3.1.4.16 2.8
-
 cyclic 2',3'-AMP wild type enzyme, in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2 Mycobacterium tuberculosis
3.1.4.16 2.95
-
 cyclic 2',3'-AMP in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2 Escherichia coli
3.1.4.16 3
-
 p-nitrophenyl phosphate in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2 Escherichia coli
3.1.4.16 12.4
-
 bis-p-nitrophenyl phosphate wild type enzyme, in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2 Mycobacterium tuberculosis
3.1.4.16 72
-
 bis-p-nitrophenyl phosphate in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2 Escherichia coli

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.1.4.16 2.5
-
-
 Escherichia coli phosphate