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Literature summary for 4.1.2.25 extracted from

  • Pribat, A.; Jeanguenin, L.; Lara-Nunez, A.; Ziemak, M.J.; Hyde, J.E.; de Crecy-Lagard, V.; Hanson, A.D.
    6-Pyruvoyltetrahydropterin synthase paralogs replace the folate synthesis enzyme dihydroneopterin aldolase in diverse bacteria (2009), J. Bacteriol., 191, 4158-4165.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli folB deletant cells Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7,8-dihydroneopterin Escherichia coli
-
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
?
7,8-dihydroneopterin Escherichia coli MG1655
-
6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli MG1655
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7,8-dihydroneopterin
-
Escherichia coli 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
?
7,8-dihydroneopterin
-
Escherichia coli MG1655 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
?

Synonyms

Synonyms Comment Organism
FolB
-
Escherichia coli

General Information

General Information Comment Organism
malfunction 6-pyruvoyltetrahydropterin synthase paralogs with an active-site glutamate (designated PTPS-III proteins) can functionally replace FolB in vivo Escherichia coli