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Literature summary for 2.7.6.3 extracted from

  • Ballantine, S.P.; Volpe, F.; Delves, C.J.
    The hydroxymethyldihydropterin pyrophosphokinase domain of the multifunctional folic acid synthesis Fas protein of Pneumocystis carinii expressed as an independent enzyme in Escherichia coli: refolding and characterization of the recombinant enzyme (1994), Protein Expr. Purif., 5, 371-378.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
the hydroxymethyldihydropterin pyrophosphokinase domain of the multifunctional folic acid synthesis Fas protein expressed as an independent enzyme in Escherichia coli, high level expression in inclusion bodies using an inducible tac promoter expression system Pneumocystis carinii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0036
-
6-hydroxymethyl-7,8-dihydropteridine pH 8.2, 50 mM Tris buffer Pneumocystis carinii
0.015
-
ATP
-
Escherichia coli
0.015
-
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine
-
Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ less effective than Mn2+ or Mg2+ in activation Escherichia coli
Mg2+ required, optimal activity at 4 mM Escherichia coli
Mn2+ can replace Mg2+ with a 10 mM optimum Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
150000
-
gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Pneumocystis carinii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Escherichia coli

Storage Stability

Storage Stability Organism
-20°C, enzyme loses activity over a period of months Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
-
Escherichia coli AMP + 2-amino-7,8-dihydro-4-hydroxy-6-(diphosphooxymethyl)pteridine
-
?
ATP + 6-hydroxymethyl-7,8-dihydropteridine
-
Pneumocystis carinii AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
-
?
dATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine
-
Escherichia coli dAMP + 2-amino-7,8-dihydro-4-hydroxy-6-(diphosphooxymethyl)pteridine
-
?

Subunits

Subunits Comment Organism
More 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase domain of the multifunctional folic acid synthesis enzyme Pneumocystis carinii

Synonyms

Synonyms Comment Organism
More 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase domain of the multifunctional folic acid synthesis enzyme Pneumocystis carinii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
100
-
60 min, 75% loss of activity Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Pneumocystis carinii
8.5
-
-
Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
7.5 10.8 active between pH 7.5 and pH 10.8 Escherichia coli

pI Value

Organism Comment pI Value Maximum pI Value
Pneumocystis carinii isoelectric focusing
-
9.1