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

BRENDA support

Literature summary extracted from

  • Keppetipola, N.; Shuman, S.
    Characterization of the 2,3 cyclic phosphodiesterase activities of Clostridium thermocellum polynucleotide kinase-phosphatase and bacteriophage lambda phosphatase (2007), Nucleic Acids Res., 35, 7721-7732.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.32 expressed in Escherichia coli Acetivibrio thermocellus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.78 H189D mutation transforms enzyme into a Mn2+-dependent phosphodiesterase devoid of monoesterase activity. Phosphodiesterase activity of mutant is strictly specific for 2',3'-cyclic phosphates which it hydrolyzes to yield a 2'-NMP as the sole product Acetivibrio thermocellus
3.1.3.32 D233E decreased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP Acetivibrio thermocellus
3.1.3.32 D236A 64% as active as wild-type Pnkp in cleaving 2',3'-cAMP Acetivibrio thermocellus
3.1.3.32 D236E decreased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP Acetivibrio thermocellus
3.1.3.32 D236N decreased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP Acetivibrio thermocellus
3.1.3.32 D392A 7-10% as active as wild type Pnkp Acetivibrio thermocellus
3.1.3.32 D392E increased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP Acetivibrio thermocellus
3.1.3.32 D392N increased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP Acetivibrio thermocellus
3.1.3.32 H189A 17% as active as wild type Pnkp Acetivibrio thermocellus
3.1.3.32 H189A decreased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP Acetivibrio thermocellus
3.1.3.32 H189D the mutation imposes strict specificity for a 2',3' cyclic phosphate, which is cleaved to form a single 2'-NMP product and shows increased activity compared to the wild type enzyme Acetivibrio thermocellus
3.1.3.32 H189E increased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP Acetivibrio thermocellus
3.1.3.32 H264A 10% as active as wild-type Pnkp in cleaving 2',3'-cAMP Acetivibrio thermocellus
3.1.3.32 H323A 60% of wild type activity Acetivibrio thermocellus
3.1.3.32 H323Q decreased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP Acetivibrio thermocellus
3.1.3.32 H376A 7-10% as active as wild type Pnkp Acetivibrio thermocellus
3.1.3.32 H376D decreased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP Acetivibrio thermocellus
3.1.3.32 H376N decreased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP Acetivibrio thermocellus
3.1.3.32 N263A 7-10% as active as wild type Pnkp Acetivibrio thermocellus
3.1.3.32 R237A 24% as active as wild-type Pnkp in cleaving 2',3'-cAMP Acetivibrio thermocellus
3.1.3.32 R237K increased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP Acetivibrio thermocellus
3.1.3.32 R237Q increased activity compared to the wild type enzyme for hydrolysis of 2',3'-cAMP Acetivibrio thermocellus
3.1.4.1 D236A strong decrease in KM value Acetivibrio thermocellus
3.1.4.1 D236N strong decrease in KM value Acetivibrio thermocellus
3.1.4.1 D392E transformation of metal specificity, mutant is a Mn2+-dependent phosphodiesterase/monoesterase Acetivibrio thermocellus
3.1.4.1 D392N transformation of metal and substrate specificity, mutant is a Mn2+-dependent phosphodiesterase Acetivibrio thermocellus
3.1.4.1 H189A transformation of metal and substrate specificity, mutant is a Mn2+-dependent phosphodiesterase Acetivibrio thermocellus
3.1.4.1 H189D transformation of metal and substrate specificity, mutant is a Mn2+-dependent phosphodiesterase. Strong stimulation of activity Acetivibrio thermocellus
3.1.4.1 H189E transformation of substrate specificity, mutant is a Mn2+/Ni2+-dependent phosphodiesterase Acetivibrio thermocellus
3.1.4.1 H189Q decrease in phosphodiesterase activity Acetivibrio thermocellus
3.1.4.1 H264A strong stimulation of phosphodiesterase activity Acetivibrio thermocellus
3.1.4.1 H264N strong stimulation of phosphodiesterase activity Acetivibrio thermocellus
3.1.4.1 H264Q strong stimulation of phosphodiesterase activity Acetivibrio thermocellus
3.1.4.1 H376D transformation of metal specificity, mutant is a Mn2+-dependent phosphodiesterase/monoesterase Acetivibrio thermocellus
3.1.4.1 H376N transformation of metal specificity, mutant is a Mn2+-dependent phosphodiesterase/monoesterase Acetivibrio thermocellus
3.1.4.1 R237A strong stimulation of phosphodiesterase activity Acetivibrio thermocellus
3.1.4.1 R237E strong stimulation of phosphodiesterase activity Acetivibrio thermocellus
3.1.4.37 D233A catalytic activity is neligible Acetivibrio thermocellus
3.1.4.37 D233E decrease in catalytic efficiency by factor 9 Acetivibrio thermocellus
3.1.4.37 D233N catalytic activity is neligible Acetivibrio thermocellus
3.1.4.37 D236A increase in enzyme affinity for substrate Acetivibrio thermocellus
3.1.4.37 D236E kinetics similar to wild-type Acetivibrio thermocellus
3.1.4.37 D236N increase in enzyme affinity for substrate Acetivibrio thermocellus
3.1.4.37 D392A decrease of both kcat and Km value Acetivibrio thermocellus
3.1.4.37 D392E 2fold increase in kcat value without affecting Km value Acetivibrio thermocellus
3.1.4.37 D392N 2fold increase in kcat value without affecting Km value Acetivibrio thermocellus
3.1.4.37 H189A slight increase of Km value with 6fold decrease in kcat value Acetivibrio thermocellus
3.1.4.37 H189D 4fold increase in kcat value without affecting Km value Acetivibrio thermocellus
3.1.4.37 H189E 2fold increase in kcat value without affecting Km value Acetivibrio thermocellus
3.1.4.37 H323A kinetics similar to wild-type Acetivibrio thermocellus
3.1.4.37 H323Q kinetics similar to wild-type Acetivibrio thermocellus
3.1.4.37 H376D 60% increase in catalytic efficiency Acetivibrio thermocellus
3.1.4.37 H376N twofold increase in catalytic efficiency Acetivibrio thermocellus
3.1.4.37 R237A 4fold increase in Km value Acetivibrio thermocellus
3.1.4.37 R237K 6fold increase in Km value Acetivibrio thermocellus
3.1.4.37 R237Q 3fold increase in Km value Acetivibrio thermocellus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.32 3.9
-
 2',3'-cAMP mutant enzyme H376D, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 4.7
-
 2',3'-cAMP mutant enzyme H376N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 6.6
-
 2',3'-cAMP mutant enzyme D236N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 7.8
-
 2',3'-cAMP mutant enzyme D236A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 18
-
 2',3'-cAMP mutant enzyme D236E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 18
-
 2',3'-cAMP mutant enzyme D392E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 18
-
 2',3'-cAMP wild type enzyme, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 20
-
 2',3'-cAMP mutant enzyme H189D, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 24
-
 2',3'-cAMP mutant enzyme H323Q, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 28
-
 2',3'-cAMP mutant enzyme H189E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 29
-
 2',3'-cAMP mutant enzyme H189A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 31
-
 2',3'-cAMP mutant enzyme D392N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 32
-
 2',3'-cAMP mutant enzyme H323A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 60
-
 2',3'-cAMP mutant enzyme R237Q, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 62
-
 2',3'-cAMP mutant enzyme D233E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 67
-
 p-Nitrophenyl phenylphosphonate wild type enzyme, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 77
-
 2',3'-cAMP mutant enzyme R237A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 100
-
 2',3'-cAMP mutant enzyme D392A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 100
-
 2',3'-cAMP mutant enzyme R237K, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.4.37 3.9
-
 cyclic 2',3'-AMP mutant H376D, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 4.7
-
 cyclic 2',3'-AMP mutant H376N, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 6.6
-
 cyclic 2',3'-AMP mutant D236N, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 7.8
-
 cyclic 2',3'-AMP mutant D236A, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 18
-
 cyclic 2',3'-AMP mutant D236E, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 18
-
 cyclic 2',3'-AMP mutant D392E, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 18
-
 cyclic 2',3'-AMP wild-type, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 20
-
 cyclic 2',3'-AMP mutant H189D, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 24
-
 cyclic 2',3'-AMP mutant H323Q, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 28
-
 cyclic 2',3'-AMP mutant H189E, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 29
-
 cyclic 2',3'-AMP mutant H189A, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 31
-
 cyclic 2',3'-AMP mutant D392N, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 32
-
 cyclic 2',3'-AMP mutant H323A, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 60
-
 cyclic 2',3'-AMP mutant R237Q, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 62
-
 cyclic 2',3'-AMP mutant D233E, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 77
-
 cyclic 2',3'-AMP mutant R237A, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 100
-
 cyclic 2',3'-AMP mutant D392A, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 100
-
 cyclic 2',3'-AMP mutant R237K, pH 7.5, 45°C Acetivibrio thermocellus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.32 Co2+ 0.5mM, supports one-third the activity of Mn2+ Acetivibrio thermocellus
3.1.3.32 Mn2+ 0.5 mM, dependent Acetivibrio thermocellus
3.1.3.32 additional information Mg2+, Ca2+, Co2+, Cd2+, Co2+, and Zn2+ have no significant influence on activity Acetivibrio thermocellus
3.1.3.32 Ni2+ 0.5mM, supports one-third the activity of Mn2+ Acetivibrio thermocellus
3.1.4.1 Mn2+ Mn2+-dependent phophomonoesterase activity requires two additional amino acid residues compared with Ni2+-dependent phosphomonoester activity. Mn2+-dependent phosphodiesterase activity requires one amino acid residues less than Ni2+-dependent phosphodiesterase activity Acetivibrio thermocellus
3.1.4.1 Ni2+ both Ni2+-dependent phophomonoesterase activity and Ni2+-dependent phosphodiesterase activity require the same seven amino acid residues of the enzyme Acetivibrio thermocellus
3.1.4.37 Mn2+ required Acetivibrio thermocellus

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.78 Acetivibrio thermocellus
-
 bifunctional polynucleotide kinase/2',3'-cyclic nucleotide phosphodiesterase
-
3.1.3.32 Acetivibrio thermocellus
-
-
-
3.1.4.1 Acetivibrio thermocellus
-
 bifunctional phosphodiesterase/phosphomonoesterase
-
3.1.4.37 Acetivibrio thermocellus
-
 polynucleotide kinase-phosphatase
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.32 Ni-agarose chromatography Acetivibrio thermocellus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.32 2',3'-cAMP + H2O
-
 Acetivibrio thermocellus ?
-
 ?
3.1.3.32 bis-p-nitrophenyl phosphate + H2O
-
 Acetivibrio thermocellus ?
-
 ?
3.1.3.32 additional information not active towards dimethyl-p-nitrophenyl phosphate, thymidine 5'-monophosphate-p-nitrophenyl ester, and p-nitrophenyl phosphorylcholine Acetivibrio thermocellus ?
-
 ?
3.1.3.32 p-nitrophenyl phenylphosphonate + H2O
-
 Acetivibrio thermocellus ?
-
 ?
3.1.4.1 2',3'-cAMP + H2O
-
 Acetivibrio thermocellus ?
-
 ?
3.1.4.1 bis-p-nitrophenyl phosphate + H2O
-
 Acetivibrio thermocellus p-nitrophenol + p-nitrophenyl phosphate processive two-step mechanism ?
3.1.4.37 cyclic 2',3'-AMP + H2O
-
 Acetivibrio thermocellus 2'-AMP
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.32 PNKP
-
 Acetivibrio thermocellus
3.1.3.32 polynucleotide kinase-phosphatase prefers a 2',3' cyclic phosphate to a 3',5'cyclic phosphate Acetivibrio thermocellus
3.1.4.37 PNKP
-
 Acetivibrio thermocellus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.3.32 additional information
-
 2',3'-cAMP mutant enzyme D236E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 0.04 1.97 2',3'-cAMP mutant enzyme R237A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 0.04 1.97 2',3'-cAMP wild type enzyme, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 0.833
-
 2',3'-cAMP mutant enzyme D392E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 0.97
-
 2',3'-cAMP mutant enzyme H189E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 1.1
-
 2',3'-cAMP mutant enzyme D392N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 1.45
-
 2',3'-cAMP mutant enzyme H189A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 1.67
-
 2',3'-cAMP mutant enzyme D392A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 3.2
-
 2',3'-cAMP mutant enzyme H376D, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 3.25
-
 2',3'-cAMP mutant enzyme D233E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 3.5
-
 2',3'-cAMP mutant enzyme R237Q, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 4.53
-
 2',3'-cAMP mutant enzyme D236A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 5.13
-
 2',3'-cAMP mutant enzyme H376N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 5.77
-
 2',3'-cAMP mutant enzyme D236N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 6.03
-
 2',3'-cAMP mutant enzyme D236E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 6.5
-
 2',3'-cAMP mutant enzyme H323Q, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 8.1
-
 2',3'-cAMP mutant enzyme R237K, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 8.55
-
 2',3'-cAMP mutant enzyme R237A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 8.93
-
 2',3'-cAMP wild type enzyme, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 9.1
-
 2',3'-cAMP mutant enzyme H323A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 15.97
-
 2',3'-cAMP mutant enzyme D392E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 17.17
-
 2',3'-cAMP mutant enzyme H189E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 18.67
-
 2',3'-cAMP mutant enzyme D392N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 20.17
-
 2',3'-cAMP mutant enzyme R237Q, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 26.17
-
 2',3'-cAMP mutant enzyme R237K, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 27.83
-
 p-Nitrophenyl phenylphosphonate wild type enzyme, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.3.32 34.33
-
 2',3'-cAMP mutant enzyme H189D, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C Acetivibrio thermocellus
3.1.4.1 0.9
-
 2',3'-cAMP pH 8.0, 45°C, mutant H264Q, presence of Ni2+ Acetivibrio thermocellus
3.1.4.1 1.7
-
 2',3'-cAMP pH 8.0, 45°C, wild-type, presence of Ni2+ Acetivibrio thermocellus
3.1.4.1 2.1
-
 2',3'-cAMP pH 8.0, 45°C, mutant H376D, presence of Mn2+ Acetivibrio thermocellus
3.1.4.1 2.5
-
 2',3'-cAMP pH 8.0, 45°C, mutant D236A, presence of Ni2+ Acetivibrio thermocellus
3.1.4.1 3 6 2',3'-cAMP pH 8.0, 45°C, mutant H189D, presence of Mn2+ Acetivibrio thermocellus
3.1.4.1 3.3
-
 2',3'-cAMP pH 8.0, 45°C, mutant H189Q, presence of Mn2+ Acetivibrio thermocellus
3.1.4.1 3.6
-
 2',3'-cAMP pH 8.0, 45°C, mutant R237K, presence of Ni2+ Acetivibrio thermocellus
3.1.4.1 3.7
-
 2',3'-cAMP pH 8.0, 45°C, mutant H189A, presence of Mn2+ Acetivibrio thermocellus
3.1.4.1 8.8
-
 2',3'-cAMP pH 8.0, 45°C, mutant D392E, presence of Mn2+ Acetivibrio thermocellus
3.1.4.1 9.3
-
 2',3'-cAMP pH 8.0, 45°C, mutant D236N, presence of Ni2+ Acetivibrio thermocellus
3.1.4.1 12
-
 2',3'-cAMP pH 8.0, 45°C, mutant H264N, presence of Ni2+ Acetivibrio thermocellus
3.1.4.1 13.8
-
 2',3'-cAMP pH 8.0, 45°C, mutant D392N, presence of Mn2+ Acetivibrio thermocellus
3.1.4.1 18
-
 2',3'-cAMP pH 8.0, 45°C, mutant H264A, presence of Ni2+ Acetivibrio thermocellus
3.1.4.1 19.3
-
 2',3'-cAMP pH 8.0, 45°C, mutant R237A, presence of Ni2+ Acetivibrio thermocellus
3.1.4.1 23.2
-
 2',3'-cAMP pH 8.0, 45°C, wild-type, presence of Mn2+ Acetivibrio thermocellus
3.1.4.1 33
-
 2',3'-cAMP pH 8.0, 45°C, mutant R237Q, presence of Ni2+ Acetivibrio thermocellus
3.1.4.1 40.5
-
 2',3'-cAMP pH 8.0, 45°C, mutant H376N, presence of Mn2+ Acetivibrio thermocellus
3.1.4.1 43.5
-
 2',3'-cAMP pH 8.0, 45°C, mutant D236A, presence of Mn2+ Acetivibrio thermocellus
3.1.4.1 52.3
-
 2',3'-cAMP pH 8.0, 45°C, mutant H264D, presence of Mn2+ Acetivibrio thermocellus
3.1.4.1 65.9
-
 2',3'-cAMP pH 8.0, 45°C, mutant D236N, presence of Mn2+ Acetivibrio thermocellus
3.1.4.1 117.5
-
 2',3'-cAMP pH 8.0, 45°C, mutant H189E, presence of Mn2+ Acetivibrio thermocellus
3.1.4.1 253
-
 2',3'-cAMP pH 8.0, 45°C, mutant H264Q, presence of Mn2+ Acetivibrio thermocellus
3.1.4.37 1.45
-
 cyclic 2',3'-AMP mutant H189A, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 1.8
-
 cyclic 2',3'-AMP mutant D392A, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 3.2
-
 cyclic 2',3'-AMP mutant H376D, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 3.25
-
 cyclic 2',3'-AMP mutant D233E, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 4.5
-
 cyclic 2',3'-AMP mutant D236A, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 5.1
-
 cyclic 2',3'-AMP mutant H376N, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 5.8
-
 cyclic 2',3'-AMP mutant D236N, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 6
-
 cyclic 2',3'-AMP mutant D236E, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 6.5
-
 cyclic 2',3'-AMP mutant H323Q, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 8.6
-
 cyclic 2',3'-AMP mutant R237A, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 8.9
-
 cyclic 2',3'-AMP wild-type, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 9.1
-
 cyclic 2',3'-AMP mutant H323A, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 15.9
-
 cyclic 2',3'-AMP mutant D392E, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 17.2
-
 cyclic 2',3'-AMP mutant H189E, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 18.7
-
 cyclic 2',3'-AMP mutant D392N, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 20.2
-
 cyclic 2',3'-AMP mutant R237Q, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 26.2
-
 cyclic 2',3'-AMP mutant R237K, pH 7.5, 45°C Acetivibrio thermocellus
3.1.4.37 34.3
-
 cyclic 2',3'-AMP mutant H189D, pH 7.5, 45°C Acetivibrio thermocellus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.32 7
-
 in the presence of Mn2+ Acetivibrio thermocellus
3.1.4.1 7.5
-
 phosphomonoesterase activity, assay at Acetivibrio thermocellus
3.1.4.1 8
-
 phosphodiesterase activity, assay at Acetivibrio thermocellus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.3.32 5.5 8 activity declines sharply at less than pH 5.5 or above pH 8.0 Acetivibrio thermocellus