Information on EC 3.1.4.56 - 7,8-dihydroneopterin 2',3'-cyclic phosphate phosphodiesterase

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The expected taxonomic range for this enzyme is: Methanocaldococcus jannaschii

EC NUMBER
COMMENTARY hide
3.1.4.56
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RECOMMENDED NAME
GeneOntology No.
7,8-dihydroneopterin 2',3'-cyclic phosphate phosphodiesterase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
7,8-dihydroneopterin 2',3'-cyclic phosphate + H2O = 7,8-dihydroneopterin 2'-phosphate
show the reaction diagram
7,8-dihydroneopterin 2',3'-cyclic phosphate + H2O = 7,8-dihydroneopterin 3'-phosphate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
6-hydroxymethyl-dihydropterin diphosphate biosynthesis II (Methanocaldococcus)
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6-hydroxymethyl-dihydropterin diphosphate biosynthesis V (Pyrococcus)
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6-hydroxymethyl-dihydropterin diphosphate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
7,8-dihydroneopterin 2',3'-cyclic phosphate 2'/3'-phosphodiesterase
Contains one zinc atom and one iron atom per subunit of the dodecameric enzyme. It hydrolyses 7,8-dihydroneopterin 2',3'-cyclic phosphate, a step in tetrahydromethanopterin biosynthesis. In vitro the enzyme forms 7,8-dihydroneopterin 2'-phosphate and 7,8-dihydroneopterin 3'-phosphate at a ratio of 4:1.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2',3'-cAMP + H2O
3'-AMP
show the reaction diagram
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?
7,8-dihydroneopterin 2',3'-cyclic phosphate + H2O
7,8-dihydroneopterin 2'-phosphate
show the reaction diagram
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
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-
?
7,8-dihydroneopterin 2',3'-cyclic phosphate + H2O
7,8-dihydroneopterin 3'-phosphate
show the reaction diagram
bis(4-nitrophenyl) phosphate + H2O
4-nitrophenyl phosphate + 4-nitrophenol
show the reaction diagram
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-
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?
O-(4-nitrophenylphosphoryl)choline + H2O
4-nitrophenyl phosphate + choline
show the reaction diagram
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?
additional information
?
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no substrates: ATP, 3',5'-cAMP, GTP, 3',5'-cGMP, and 4',5'-cFMN
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
7,8-dihydroneopterin 2',3'-cyclic phosphate + H2O
7,8-dihydroneopterin 3'-phosphate
show the reaction diagram
Q58247
the enzyme is involved in methanopterin biosynthesis
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
0.75 mM Mn2+ shows a 6fold activation of hydrolysis of bis(4-nitrophenyl) phosphate
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
Mn2+
0.75 mM Mn2+ shows a 215fold activation of hydrolysis of bis(4-nitrophenyl) phosphate
Ni2+
0.75 mM Mn2+ shows a 1.5fold activation of hydrolysis of bis(4-nitrophenyl) phosphate
additional information
no activation of hydrolysis of bis(4-nitrophenyl) phosphate by Mg2+, Zn2+ or Fe3+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.003
0.75 mM Ni2, pH 7.2, 70C, hydrolysis of bis(4-nitrophenyl) phosphate
0.012
0.75 mM Co2+, pH 7.2, 70C, hydrolysis of bis(4-nitrophenyl) phosphate
0.029
1.4 mM Fe2+, pH 7.2, 70C, hydrolysis of 7,8-dihydroneopterin 2',3'-cyclic phosphate
0.37
0.75 mM Fe2+, pH 7.2, 70C, hydrolysis of bis(4-nitrophenyl) phosphate
0.43
0.75 mM Mn2+, pH 7.2, 70C, hydrolysis of bis(4-nitrophenyl) phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
pH 6.5: about 50% of maximal activity, pH 8.5: about 45% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28500
12 * 28500, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homododecamer
12 * 28500, calculated from sequence; 12 * 29000-30000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70 - 100
after heating for 45 min in absence of Mn2+ the activity of the enzyme drops about 30% from the 70C heated sample to the 100C heated sample. In the presence of Mn2+, in the case of 45 min heating the activity of the enzyme increases about 53%from the 70C heated sample to the 100C heated sample. In the case of 2.5 h heating the activity of the enzyme drops about 26% from the 70C heated sample to the 100C heated sample. Adding Mn2+ to the enzyme increases the temperature stability of the protein
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen inactivation with a half-life of about 5 min
718857
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D167N
reduced activities when assayed with bis(4-nitrophenyl) phosphate, 2',3'-cAMP or 7,8-dihydroneopterin 2',3'-cyclic phosphate
H61N
reduced activities when assayed with bis(4-nitrophenyl) phosphate, 2',3'-cAMP or 7,8-dihydroneopterin 2',3'-cyclic phosphate
H96N
mutant shows about 1.9-fold higher specific activity with bis(4-nitrophenyl) phosphate than that of the wild type