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Literature summary for 4.1.2.25 extracted from

  • Volpe, F.; Ballantine, S.P.; Delves, C.J.
    Two domains with amino-acid sequence similarity are required for dihydroneopterin aldolase function in the multifunctional folic acid synthesis Fas protein of Pneumocystis carnii (1995), Gene, 160, 41-46.
    View publication on PubMed
Search for more literature for 4.1.2.25

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0023
-
 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine
-
 Pneumocystis carinii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine Pneumocystis carinii first enzyme in the folate synthesis pathway ?
-
 ?

Organism

Organism UniProt Comment Textmining
Pneumocystis carinii
-
 multifunctional Fas enzyme with the activity of the first three enzymes of the folate synthesis pathway: dihydroneopterin aldolase, hydroxymethyldihydropterin pyrophosphokinase and dihydropteroate synthase
-

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
-
 Pneumocystis carinii 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
-
 ?
2-Amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine first enzyme in the folate synthesis pathway Pneumocystis carinii ?
-
 ?

Subunits

Subunits Comment Organism
More FasA and FasB may be two subunits of the dihydroneopterin aldolase enzyme moiety within the multifunctional Fas protein Pneumocystis carinii