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Literature summary extracted from

  • Thomas, M.C.; Ballantine, S.P.; Bethell, S.S.; Bains, S.; Kellam, P.; Delves, C.J.
    Single amino acid substitutions dirupts tetramer formation in the dihydroneopterin aldolase enzyme of Pneumocystis carnii (1998), Biochemistry, 37, 11629-11636.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.2.25 overproduced as an independent monofunctional activity in Escherichia coli, FasAB-Met23 Pneumocystis carinii

Protein Variants

EC Number Protein Variants Comment Organism
4.1.2.25 D39E FasA domain mutant D39E and FasB domain mutant G175A have no detectable activity of dihydroneopterin aldolase. The FasA domain mutants, G53A and Q63N and the FasB domain mutant Q185N, show approximately 11-fold, 16-fold and 24-fold decrease, respectively, in specific activity compared to wild-type FasAB-Met23. The activity of the FasB domain mutant D161E is similar to that of wild-type enzyme. The two mutant enzymes K96R and K218R have levels of activity comparable to wild-type enzyme Pneumocystis carinii
4.1.2.25 G175A FasA domain mutant D39E and FasB domain mutant G175A have no detectable activity of dihydroneopterin aldolase. The FasA domain mutants, G53A and Q63N and the FasB domain mutant Q185N, show approximately 11-fold, 16-fold and 24-fold decrease, respectively, in specific activity compared to wild-type FasAB-Met23. The activity of the FasB domain mutant D161E is similar to that of wild-type enzyme. The two mutant enzymes K96R and K218R have levels of activity comparable to wild-type enzyme Pneumocystis carinii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.2.25 29689
-
 4 * 29689, independent monofunctional activity FasAB-Met23, mass spectrometry Pneumocystis carinii
4.1.2.25 119000
-
 independent monofunctional activity FasAB-Met23, gel filtration Pneumocystis carinii

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.25 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
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.2.25 native and recombinant independent monofunctional activity FasAB-Met23 Pneumocystis carinii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.25 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
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.2.25 tetramer 4 * 29689, independent monofunctional activity FasAB-Met23, mass spectrometry Pneumocystis carinii