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Literature summary for 3.1.4.16 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)

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

Protein Variants

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

Inhibitors

Inhibitors Comment Organism Structure
phosphate
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
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
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
6
-
p-nitrophenyl phosphate in Tris-HCl buffer (pH 8.5) in the presence of 5 mM MnCl2 Escherichia coli
9.3
-
bis-p-nitrophenyl phosphate in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2 Escherichia coli
35
-
cyclic 2',3'-AMP in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2 Escherichia coli

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P67095
-
-
Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
bis-p-nitrophenyl phosphate + H2O
-
Mycobacterium tuberculosis p-nitrophenol + p-nitrophenyl phosphate
-
?
bis-p-nitrophenyl phosphate + H2O
-
Escherichia coli p-nitrophenol + p-nitrophenyl phosphate
-
?
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
-
?
cyclic 2',3'-AMP + H2O YfcE-C74H cleaves exclusively the P-O2' bond of 2',3'-cAMP Escherichia coli 3'-AMP
-
?
cyclic 2',3'-GMP + H2O
-
Mycobacterium tuberculosis 3'-GMP
-
?
cyclic 2',3'-GMP + H2O
-
Escherichia coli 3'-GMP
-
?
cyclic 3',5'-AMP + H2O weak activity Escherichia coli 5'-AMP
-
?
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
-
?
cyclic 3',5'-GMP + H2O weak activity Mycobacterium tuberculosis 5'-GMP
-
?
cyclic 3',5'-GMP + H2O weak activity Escherichia coli 5'-GMP
-
?
cyclic 3',5'-UMP + H2O weak activity Mycobacterium tuberculosis 5'-UMP
-
?
cyclic 3',5'-UMP + H2O weak activity Escherichia coli 5'-UMP
-
?
additional information the enzyme does not have a preference for 2',3'-cAMP versus 2',3'-cGMP Mycobacterium tuberculosis ?
-
?
additional information YfcE-C74H has no detectable ability to hydrolyze phosphomonoester substrates 5'-AMP, 3'-AMP, or 2'-AMP Escherichia coli ?
-
?
p-nitrophenyl phosphate + H2O
-
Escherichia coli p-nitrophenol + phosphate
-
?
p-nitrophenyl phosphate + H2O weak activity Mycobacterium tuberculosis p-nitrophenol + phosphate
-
?

Synonyms

Synonyms Comment Organism
2,3-cyclic nucleotide phosphodiesterase
-
Mycobacterium tuberculosis
Rv0805 functions as a 3',5'-cyclic nucleotide phosphodiesterase but has also 2',3'-cyclic nucleotide phosphodiesterase function Mycobacterium tuberculosis
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]

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

IC50 Value

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