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Literature summary extracted from

  • Mashhadi, Z.; Xu, H.; White, R.H.
    An Fe2+-dependent cyclic phosphodiesterase catalyzes the hydrolysis of 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate in methanopterin biosynthesis (2009), Biochemistry, 48, 9384-9392.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.4.56 expression in Escherichia coli Methanocaldococcus jannaschii

Protein Variants

EC Number Protein Variants Comment Organism
3.1.4.56 D167N reduced activities when assayed with bis(4-nitrophenyl) phosphate, 2',3'-cAMP or 7,8-dihydroneopterin 2',3'-cyclic phosphate Methanocaldococcus jannaschii
3.1.4.56 H61N reduced activities when assayed with bis(4-nitrophenyl) phosphate, 2',3'-cAMP or 7,8-dihydroneopterin 2',3'-cyclic phosphate Methanocaldococcus jannaschii
3.1.4.56 H96N mutant shows about 1.9-fold higher specific activity with bis(4-nitrophenyl) phosphate than that of the wild type Methanocaldococcus jannaschii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.4.56 Co2+ 0.75 mM Mn2+ shows a 6fold activation of hydrolysis of bis(4-nitrophenyl) phosphate Methanocaldococcus jannaschii
3.1.4.56 Fe2+ the enzyme contains one atom of both zinc and iron per protomer. The enzyme requires Fe2+ for activity. After the addition of 1.4 mM Fe2+ the enzyme shows a specific activity of 29 nmol/min*mg for the hydrolysis of 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate. 0.75 mM Fe2+ shows a 185fold activation of hydrolysis of bis(4-nitrophenyl) phosphate Methanocaldococcus jannaschii
3.1.4.56 Mn2+ 0.75 mM Mn2+ shows a 215fold activation of hydrolysis of bis(4-nitrophenyl) phosphate Methanocaldococcus jannaschii
3.1.4.56 additional information no activation of hydrolysis of bis(4-nitrophenyl) phosphate by Mg2+, Zn2+ or Fe3+ Methanocaldococcus jannaschii
3.1.4.56 Ni2+ 0.75 mM Mn2+ shows a 1.5fold activation of hydrolysis of bis(4-nitrophenyl) phosphate Methanocaldococcus jannaschii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.4.56 28500
-
 12 * 28500, calculated from sequence Methanocaldococcus jannaschii
3.1.4.56 370000
-
 gel filtration Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.4.56 7,8-dihydroneopterin 2',3'-cyclic phosphate + H2O Methanocaldococcus jannaschii the enzyme is involved in methanopterin biosynthesis 7,8-dihydroneopterin 3'-phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.56 Methanocaldococcus jannaschii Q58247
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
3.1.4.56 oxygen inactivation with a half-life of about 5 min Methanocaldococcus jannaschii

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.4.56
-
 Methanocaldococcus jannaschii

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.4.56 7,8-dihydroneopterin 2',3'-cyclic phosphate + H2O = 7,8-dihydroneopterin 2'-phosphate (2) Methanocaldococcus jannaschii
a
3.1.4.56 7,8-dihydroneopterin 2',3'-cyclic phosphate + H2O = 7,8-dihydroneopterin 3'-phosphate (1) Methanocaldococcus jannaschii
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.4.56 0.003
-
 0.75 mM Ni2, pH 7.2, 70°C, hydrolysis of bis(4-nitrophenyl) phosphate Methanocaldococcus jannaschii
3.1.4.56 0.012
-
 0.75 mM Co2+, pH 7.2, 70°C, hydrolysis of bis(4-nitrophenyl) phosphate Methanocaldococcus jannaschii
3.1.4.56 0.029
-
 1.4 mM Fe2+, pH 7.2, 70°C, hydrolysis of 7,8-dihydroneopterin 2',3'-cyclic phosphate Methanocaldococcus jannaschii
3.1.4.56 0.37
-
 0.75 mM Fe2+, pH 7.2, 70°C, hydrolysis of bis(4-nitrophenyl) phosphate Methanocaldococcus jannaschii
3.1.4.56 0.43
-
 0.75 mM Mn2+, pH 7.2, 70°C, hydrolysis of bis(4-nitrophenyl) phosphate Methanocaldococcus jannaschii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.56 2',3'-cAMP + H2O
-
 Methanocaldococcus jannaschii 3'-AMP
-
 ?
3.1.4.56 7,8-dihydroneopterin 2',3'-cyclic phosphate + H2O the enzyme is involved in methanopterin biosynthesis Methanocaldococcus jannaschii 7,8-dihydroneopterin 3'-phosphate
-
 ?
3.1.4.56 7,8-dihydroneopterin 2',3'-cyclic phosphate + H2O the enzyme hydrolyses 7,8-dihydroneopterin 2',3'-cyclic phosphate and converts it to a mixture of 7,8-dihydroneopterin 3'-phosphate and 7,8-dihydroneopterin 2'-phosphate. In vitro the ratio of 7,8-dihydroneopterin 3'-phosphate to 7,8-dihydroneopterin 2'-phosphate is 1:4 Methanocaldococcus jannaschii 7,8-dihydroneopterin 3'-phosphate
-
 ?
3.1.4.56 7,8-dihydroneopterin 2',3'-cyclic phosphate + H2O the enzyme hydrolyses 7,8-dihydroneopterin 2',3'-cyclic phosphate and converts it to a mixture of 7,8-dihydroneopterin 3'-phosphate and 7,8-dihydroneopterin 2'-phosphate. In vitro the ratio of 7,8-dihydroneopterin 3'-phosphate to 7,8-dihydroneopterin 2'-phosphate is 1:4 Methanocaldococcus jannaschii 7,8-dihydroneopterin 2'-phosphate
-
 ?
3.1.4.56 bis(4-nitrophenyl) phosphate + H2O
-
 Methanocaldococcus jannaschii 4-nitrophenyl phosphate + 4-nitrophenol
-
 ?
3.1.4.56 additional information no substrates: ATP, 3',5'-cAMP, GTP, 3',5'-cGMP, and 4',5'-cFMN Methanocaldococcus jannaschii ?
-
 ?
3.1.4.56 O-(4-nitrophenylphosphoryl)choline + H2O
-
 Methanocaldococcus jannaschii 4-nitrophenyl phosphate + choline
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.4.56 homododecamer 12 * 28500, calculated from sequence Methanocaldococcus jannaschii
3.1.4.56 homododecamer 12 * 29000-30000, SDS-PAGE Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
3.1.4.56 MJ0837 gene product
-
 Methanocaldococcus jannaschii
3.1.4.56 MptB
-
 Methanocaldococcus jannaschii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.4.56 70
-
 assay at Methanocaldococcus jannaschii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.4.56 70 100 after heating for 45 min in absence of Mn2+ the activity of the enzyme drops about 30% from the 70°C heated sample to the 100°C heated sample. In the presence of Mn2+, in the case of 45 min heating the activity of the enzyme increases about 53%from the 70°C heated sample to the 100°C heated sample. In the case of 2.5 h heating the activity of the enzyme drops about 26% from the 70°C heated sample to the 100°C heated sample. Adding Mn2+ to the enzyme increases the temperature stability of the protein Methanocaldococcus jannaschii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.4.56 7.2
-
 assay at Methanocaldococcus jannaschii
3.1.4.56 7.5
-
 CHES buffer Methanocaldococcus jannaschii

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.4.56 6.5 8.5 pH 6.5: about 50% of maximal activity, pH 8.5: about 45% of maximal activity Methanocaldococcus jannaschii