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Literature summary extracted from

  • Mouillon, J.M.; Ravanel, S.; Douce, R.; Rebeille, F.
    Folate synthesis in higher-plant mitochondria: coupling between the dihydropterin pyrophosphokinase and the dihydropteroate synthase activities (2002), Biochem. J., 363, 313-319.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.15 expression of recombinant enzyme in Escherichia coli Pisum sativum
2.7.6.3 bifunctional protein 6-hydroxymethyl-7,8-dihydroxypterin pyrophosphokinase/7,8-dihydropteroate synthase is involved in tetrahydrofolate expressed in Escherichia coli Pisum sativum

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.15 7,8-Dihydropteroic acid
-
Pisum sativum
2.5.1.15 dihydrofolate monoglutamate
-
Pisum sativum
2.5.1.15 tetrahydrofolate monoglutamate
-
Pisum sativum
2.7.6.3 6-hydroxymethyl-7,8-dihydropterin diphosphate competitive inhibitor of ATP, mixed type inhibitor of 6-hydroxymethyl-7,8-dihydropteridine Pisum sativum
2.7.6.3 AMP poor inhibitor Pisum sativum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.15 additional information
-
additional information activity in plant enzyme and recombinant enzyme Pisum sativum
2.7.6.3 0.001
-
6-hydroxymethyl-7,8-dihydropteridine bifunctional enzyme 6-hydroxymethyl-7,8-dihydroxypterin pyrophosphokinase/7,8-dihydropteroate synthase Pisum sativum
2.7.6.3 0.002
-
6-hydroxymethyl-7,8-dihydropteridine recombinant bifunctional enzyme 6-hydroxymethyl-7,8-dihydroxypterin pyrophosphokinase/7,8-dihydropteroate synthase expressed in Escherichia coli Pisum sativum
2.7.6.3 0.07
-
ATP bifunctional enzyme 6-hydroxymethyl-7,8-dihydroxypterin pyrophosphokinase/7,8-dihydropteroate synthase from Pisum sativum and recombinant enzyme expressed in Escherichia coli Pisum sativum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.5.1.15 mitochondrion
-
Pisum sativum 5739
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.15 53000
-
SDS-PAGE analysis of soluble protein Pisum sativum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.15 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate Pisum sativum
-
diphosphate + 7,8-dihydropteroate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.15 Pisum sativum
-
-
-
2.7.6.3 Pisum sativum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.15 recombinant enzyme, affinity column Pisum sativum
2.7.6.3 recombinant bifunctional protein 6-hydroxymethyl-7,8-dihydroxypterin pyrophosphokinase/7,8-dihydropteroate synthase is involved in tetrahydrofolate Pisum sativum

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.5.1.15 leaf
-
Pisum sativum
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.5.1.15 additional information
-
specific activity in plant enzyme and recombinant enzyme Pisum sativum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.15 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
-
Pisum sativum diphosphate + 7,8-dihydropteroate
-
?
2.7.6.3 ATP + 6-hydroxymethyl-7,8-dihydropteridine ordered bi bi mechanism where ATP binds first and 6-hydroxymethyl-7,8-dihydropterin diphosphate is released last Pisum sativum AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
-
?

Subunits

EC Number Subunits Comment Organism
2.7.6.3 More the bifunctional protein 6-hydroxymethyl-7,8-dihydroxypterin pyrophosphokinase/7,8-dihydropteroate synthase is involved in tetrahydrofolate synthesis Pisum sativum

Synonyms

EC Number Synonyms Comment Organism
2.7.6.3 6-hydroxymethyl-7,8-dihydroxypterin pyrophosphokinase/7,8-dihydropteroate synthase bifunctional protein involved in tetrahydrofolate synthesis Pisum sativum
2.7.6.3 HPPK/DHPS
-
Pisum sativum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.15 30
-
assay at Pisum sativum

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.5.1.15 additional information
-
additional information KI values of folate derivatives Pisum sativum
2.7.6.3 0.005
-
6-hydroxymethyl-7,8-dihydropterin diphosphate versus ATP Pisum sativum
2.7.6.3 0.013
-
6-hydroxymethyl-7,8-dihydropterin diphosphate versus 6-hydroxymethyl-7,8-dihydropteridine Pisum sativum
2.7.6.3 0.4
-
AMP versus 6-hydroxymethyl-7,8-dihydropteridine Pisum sativum
2.7.6.3 0.7
-
AMP versus ATP Pisum sativum