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Literature summary extracted from

  • Wang, Y.; Li, Y.; Wu, Y.; Yan, H.
    Mechanism of dihydroneopterin aldolase. NMR, equilibrium and transient kinetic studies of the Staphylococcus aureus and Escherichia coli enzymes (2007), FEBS J., 274, 2240-2252.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.2.25 expressed in Escherichia coli BL21(DE3) cells Staphylococcus aureus
4.1.2.25 expressed in Escherichia coli BL21(DE3) cells Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.2.25 10
-
glycoaldehyde apparent value Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.25 Escherichia coli
-
-
-
4.1.2.25 Staphylococcus aureus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.2.25 Ni-nitrilotriacetate column chromatography, DEAE-cellulose column chromatography and Bio-Gel A-0.5 m gel filtration Staphylococcus aureus
4.1.2.25 Ni-nitrilotriacetate column chromatography, DEAE-cellulose column chromatography and Bio-Gel A-0.5 m gel filtration Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.25 7,8-dihydroneopterin
-
Staphylococcus aureus 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
r
4.1.2.25 7,8-dihydroneopterin
-
Escherichia coli 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
-
r

Synonyms

EC Number Synonyms Comment Organism
4.1.2.25 DHNA DHNA catalyzes both the cleavage of 7,8-dihydroneopterin to form 6-hydroxymethyl-7,8-dihydropterin and glycolaldehyde and the epimerization of 7,8-dihydroneopterin to form 7,8-dihydro-l-monapterin Staphylococcus aureus
4.1.2.25 DHNA DHNA catalyzes both the cleavage of 7,8-dihydroneopterin to form 6-hydroxymethyl-7,8-dihydropterin and glycolaldehyde and the epimerization of 7,8-dihydroneopterin to form 7,8-dihydro-l-monapterin Escherichia coli