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Literature summary for 3.6.1.67 extracted from

  • Suzuki, Y.; Brown, G.M.
    The biosynthesis of folic acid. XII. Purification and properties of dihydroneopterin triphosphate pyrophosphohydrolase (1974), J. Biol. Chem., 249, 2405-2410.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
7,8-dihydroneopterin 3'-phosphate 0.074 mM, 21% inhibition; inhibits 21% at a concentration of 0.074 mM, when the substrate is present at 0.032 mM Escherichia coli
diphosphate 1 mM, 89% inhibition Escherichia coli
dTTP 1 mM, 72% inhibition Escherichia coli
additional information no inhibition by dihydrofolic acid, dihydropteroic acid, dihydroneopterin and 6-hydroxy-methyl-dihydropterin Escherichia coli
TTP 1 mM, 72% inhibition Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.011
-
7,8-dihydroneopterin 3'-triphosphate pH 8.5, 42°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ divalent cations are rerquired for the enzyme to function. Maximal activation is achieved with 8 mM Mg2+. Zn2+ and Ca2+ (both at 8 mM) are 2.4% and 7.1%, respectively, as effective as Mg2+. Mn2+ can not be tested because 7,8-dihydroneopterin triphosphate is rapidly and nonenzymatically decomposed in the presence of Mn2+ Escherichia coli
Mg2+ maximal activation is achieved with 8 nM Mg2+. Zn2+ and Ca2+ (both at 8 mM) are 2.4% and 7.1%, respectively, as effective as Mg2 Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
17000
-
-
Escherichia coli
17000
-
gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7,8-dihydroneopterin 3'-triphosphate + H2O Escherichia coli the enzyme participates in a folate biosynthesis pathway 7,8-dihydroneopterin 3'-phosphate + diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli P0AFC0
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7,8-dihydroneopterin 3'-triphosphate + H2O
-
Escherichia coli 7,8-dihydroneopterin 3'-phosphate + diphosphate
-
?
7,8-dihydroneopterin 3'-triphosphate + H2O the enzyme participates in a folate biosynthesis pathway Escherichia coli 7,8-dihydroneopterin 3'-phosphate + diphosphate
-
?
additional information no activity with ATP, GTP, dihydroneopterin phosphate, 4-nitrophenyl hosphate or diphosphate Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
dihydroneopterin triphosphate pyrophosphohydrolase
-
Escherichia coli
H2-neopterin-PPP pyrophosphohydrolase
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
42
-
-
Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
10
-
1 min, activity is destroyed Escherichia coli
100
-
1 min, enzyme is destroyed Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
7.1 9.7 half-maximal activity at pH.1 and at pH 9.7 Escherichia coli
7.1 9.7 half-maximal activity at pH 7.1 and at pH 9.7 Escherichia coli

General Information

General Information Comment Organism
metabolism the enzyme participates in a folate biosynthesis pathway Escherichia coli