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Literature summary for 2.7.6.3 extracted from

  • Gao, K.; He, H.; Yang, M.; Yan, H.
    Molecular dynamics simulations of the Escherichia coli HPPK apo-enzyme reveal a network of conformational transitions (2015), Biochemistry, 54, 6734-6742.
    View publication on PubMed
Search for more literature for 2.7.6.3

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine Escherichia coli
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 AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P26281
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate during its catalytic cycle, the enzyme must assume at least five liganded forms: the apoenzyme form (without either of the substrates), the binary substrate complex with MgATP, the ternary substrate complex (Michaelis complex) with MgATP and 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine, the ternary product complex with AMP and 6-hydroxymethyl-7,8-dihydropterin diphosphate (HPPP), and the binary product complex with HPPP Escherichia coli
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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-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
-
 ?

Subunits

Subunits Comment Organism
More the enzyme has an alphabetaalpha fold with a central six-stranded beta-sheet sandwiched by two alpha-helices on either side Escherichia coli

Synonyms

Synonyms Comment Organism
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
-
 Escherichia coli
HPPK
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 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli

General Information

General Information Comment Organism
metabolism 6-hydroxymethyl-7,8-dihydropterin diphosphokinase catalyzes the first reaction in the folate biosynthetic pathway Escherichia coli
additional information putative large-scale induced-fit conformational change of enzyme HPPK. The loops 2 and 3 remain rather flexible when the enzyme is in its apoform, but loops 2 and 3 adopt the open, semi-open, and closed conformations throughout its catalytic cycle, flexibility of the three catalytic loops in the apoform of the enzyme. Molecular dynamics simulations of the apoenzyme at two different temperatures, overview Escherichia coli
physiological function the enzyme is essential for microbial growth Escherichia coli