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Literature summary for 4.1.2.25 extracted from

  • Garcon, A.; Levy, C.; Derrick, J.P.
    Crystal structure of the bifunctional dihydroneopterin aldolase/6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase from Streptococcus pneumoniae (2006), J. Mol. Biol., 360, 644-653.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 (DE3) cells Streptococcus pneumoniae

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapour diffusion method with 50 mM MOPS/NaOH (pH 7.0), 17.5% (w/v) methoxy-PEG 2000, 400 mM NaCl, 10 mM MgCl2, 2 mM dithiothreitol, 1 mM EDTA and 5% (v/v) glycerol Streptococcus pneumoniae

Organism

Organism UniProt Comment Textmining
Streptococcus pneumoniae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Mono Q 10/10 column chromatography, Superdex 200 gel filtration Streptococcus pneumoniae

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
octamer x-ray crystallography Streptococcus pneumoniae
tetramer active enzyme in solution Streptococcus pneumoniae

Synonyms

Synonyms Comment Organism
DHNA-HPPK DHNA is part of the bifunctional dihydroneopterin aldolase/6 hydroxymethyl-7,8-dihydropterin pyrophosphokinase, also called SulD Streptococcus pneumoniae