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Literature summary for 5.1.99.8 extracted from

  • Hau¯mann, C.; Rohdich, F.; Schmidt, E.; Bacher, A.; Richter, G.
    Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase (1998), J. Biol. Chem., 273, 17418-17424.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.013
-
7,8-dihydroneopterin triphosphate pH 8.0, 55°C Escherichia coli
0.066
-
7,8-dihydromonapterin pH 8.0, 55°C Escherichia coli
0.149
-
7,8-dihydroneopterin pH 8.0, 55°C Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
13988
-
8 * 13988, calculated, 8 * 14000, SDS-PAGE Escherichia coli
14000
-
8 * 13988, calculated, 8 * 14000, SDS-PAGE Escherichia coli
111600
-
sedimentation equilibrium analysis Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AC19
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.8
-
pH 8.0, 55°C Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7,8-dihydromonapterin
-
Escherichia coli 7,8-dihydroneopterin
-
?
7,8-dihydroneopterin
-
Escherichia coli 7,8-dihydromonapterin
-
r
7,8-dihydroneopterin triphosphate
-
Escherichia coli 7,8-dihydromonapterin triphosphate
-
r
additional information catalyzes the epimerization of carbon 2' in the triphosphates of dihydroneopterin and dihydromonapterin. The enzyme can also catalyze the cleavage of the position 6 side chain of several pteridine derivatives at a slow rate Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
octamer 8 * 13988, calculated, 8 * 14000, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
folX
-
Escherichia coli

General Information

General Information Comment Organism
physiological function a folX deletion mutant has normal growth properties on complete medium as well as on minimal medium Escherichia coli