Literature summary for 4.1.2.25 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.

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Cloned(Commentary)

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

Protein Variants

Protein Variants	Comment	Organism
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
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]

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

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	-

Purification (Commentary)

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

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	-	?

Subunits

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

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Release 2023.1 (January 2023)