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Literature summary for 2.7.6.3 extracted from

  • Yun, M.K.; Hoagland, D.; Kumar, G.; Waddell, M.B.; Rock, C.O.; Lee, R.E.; White, S.W.
    The identification, analysis and structure-based development of novel inhibitors of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (2014), Bioorg. Med. Chem., 22, 2157-2165.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.6.3

Application

Application Comment Organism
drug development the enzyme is a target for antimicrobial development Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information the enzyme is minimally biotinylated by reaction with EZ-Link sulfo-NHS-LC-LC-biotin Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
2-amino-8-(2-oxo-2-phenylethoxy)-1,4,5,9-tetrahydro-6H-purin-6-one
-
 Escherichia coli
2-amino-8-hydroxy-1,4,5,9-tetrahydro-6H-purin-6-one
-
 Escherichia coli
2-amino-8-[2-(2-methylphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
-
 Escherichia coli
2-amino-8-[2-(3-methylphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
-
 Escherichia coli
2-amino-8-[2-(4-fluorophenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
-
 Escherichia coli
2-amino-8-[2-(4-hydroxyphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
-
 Escherichia coli
2-amino-8-[2-(4-methoxyphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
-
 Escherichia coli
2-amino-8-[2-(4-methylphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
-
 Escherichia coli
4-[(2-amino-6-oxo-4,5,6,9-tetrahydro-1H-purin-8-yl)methyl]benzonitrile
-
 Escherichia coli
4-[[(2-amino-6-oxo-4,5,6,9-tetrahydro-1H-purin-8-yl)oxy]acetyl]benzonitrile
-
 Escherichia coli
additional information identification of several enzyme inhibitors that contain an aryl substituted 8-thioguanine scaffold. The compounds engage the enzyme pterin-binding pocket and an induced cryptic pocket, preliminary structure activity relationship profile, binding structures, overview Escherichia coli

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
-
 AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P26281 gene folK
-

Reaction

Reaction Comment Organism Reaction ID
ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate in the enzyme mechanism, the assembly of the pterin-binding pocket depends on ATP-dependent conformational changes in the three active site loops Escherichia coli
a

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
-
 ?

Synonyms

Synonyms Comment Organism
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
-
 Escherichia coli
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
-
 Escherichia coli
HPPK
-
 Escherichia coli
PPPK
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
23
-
 assay at Escherichia coli

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli

General Information

General Information Comment Organism
metabolism essential enzyme in the microbial folate biosynthetic pathway Escherichia coli
additional information movements of Arg82 and Arg92 adjacent to the phosphate groups of the bound ATP play an essential role in HPPK catalysis Escherichia coli
physiological function essential enzyme in the microbial folate biosynthetic pathway Escherichia coli