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Literature summary for 3.1.4.56 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)

Cloned (Comment) Organism
expression in Escherichia coli Methanocaldococcus jannaschii

Protein Variants

Protein Variants Comment Organism
D167N reduced activities when assayed with bis(4-nitrophenyl) phosphate, 2',3'-cAMP or 7,8-dihydroneopterin 2',3'-cyclic phosphate Methanocaldococcus jannaschii
H61N reduced activities when assayed with bis(4-nitrophenyl) phosphate, 2',3'-cAMP or 7,8-dihydroneopterin 2',3'-cyclic phosphate Methanocaldococcus jannaschii
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

Metals/Ions Comment Organism Structure
Co2+ 0.75 mM Mn2+ shows a 6fold activation of hydrolysis of bis(4-nitrophenyl) phosphate Methanocaldococcus jannaschii
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
Mn2+ 0.75 mM Mn2+ shows a 215fold activation of hydrolysis of bis(4-nitrophenyl) phosphate Methanocaldococcus jannaschii
additional information no activation of hydrolysis of bis(4-nitrophenyl) phosphate by Mg2+, Zn2+ or Fe3+ Methanocaldococcus jannaschii
Ni2+ 0.75 mM Mn2+ shows a 1.5fold activation of hydrolysis of bis(4-nitrophenyl) phosphate Methanocaldococcus jannaschii

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii Q58247
-
-

Oxidation Stability

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

Purification (Commentary)

Purification (Comment) Organism
-
Methanocaldococcus jannaschii

Reaction

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2',3'-cAMP + H2O
-
Methanocaldococcus jannaschii 3'-AMP
-
?
7,8-dihydroneopterin 2',3'-cyclic phosphate + H2O the enzyme is involved in methanopterin biosynthesis Methanocaldococcus jannaschii 7,8-dihydroneopterin 3'-phosphate
-
?
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
-
?
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
-
?
bis(4-nitrophenyl) phosphate + H2O
-
Methanocaldococcus jannaschii 4-nitrophenyl phosphate + 4-nitrophenol
-
?
additional information no substrates: ATP, 3',5'-cAMP, GTP, 3',5'-cGMP, and 4',5'-cFMN Methanocaldococcus jannaschii ?
-
?
O-(4-nitrophenylphosphoryl)choline + H2O
-
Methanocaldococcus jannaschii 4-nitrophenyl phosphate + choline
-
?

Subunits

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

Synonyms

Synonyms Comment Organism
MJ0837 gene product
-
Methanocaldococcus jannaschii
MptB
-
Methanocaldococcus jannaschii

Temperature Optimum [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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

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

pH Range

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