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Literature summary for 4.1.2.25 extracted from

  • Mathis, J.B.; Brown, G.M.
    Dihydroneopterin aldolase from Escherichia coli (1980), Methods Enzymol., 66, 556-560.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
EDTA increases activity Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
2-Amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine competitive Escherichia coli
6-Formyl-dihydropterin
-
Escherichia coli
6-Methyl-dihydropterin
-
Escherichia coli
dihydrofolic acid slight Escherichia coli
Dihydropteroic acid slight Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.009
-
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
-
Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
100000
-
x * 100000, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0039
-
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine not reversible Escherichia coli 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
-
?

Subunits

Subunits Comment Organism
? x * 100000, SDS-PAGE Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.6
-
-
Escherichia coli