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EC Tree
IUBMB Comments The enzyme, which participates in a pathway for folate biosynthesis, is found in the Stramenopiles, a large group that includes oomycetes, various microalgae and brown algae, as well as in several bacterial phyla. It provides a bypass mechanism compensating for the lack of EC 4.1.2.25, dihydroneopterin aldolase. In the malaria parasite Plasmodium falciparum the enzyme is bifunctional and also catalyses the activity of EC 4.2.3.12, 6-pyruvoyltetrahydropterin synthase. cf. EC 4.1.2.59, dihydroneopterin phosphate aldolase.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
6-pyruvoyltetrahydropterin synthase, DHNA, dihydroneopterin aldolase, PTPS, PTPS-III,
more
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6-pyruvoyltetrahydropterin synthase
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dihydroneopterin aldolase
DHNA
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dihydroneopterin aldolase
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dihydroneopterin aldolase
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PTPS-III
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7,8-dihydroneopterin 3'-triphosphate = 6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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7,8-dihydroneopterin 3'-triphosphate glycolaldehyde phosphate-lyase [6-(hydroxymethyl)-7,8-dihydropterin-forming]
The enzyme, which participates in a pathway for folate biosynthesis, is found in the Stramenopiles, a large group that includes oomycetes, various microalgae and brown algae, as well as in several bacterial phyla. It provides a bypass mechanism compensating for the lack of EC 4.1.2.25, dihydroneopterin aldolase. In the malaria parasite Plasmodium falciparum the enzyme is bifunctional and also catalyses the activity of EC 4.2.3.12, 6-pyruvoyltetrahydropterin synthase. cf. EC 4.1.2.59, dihydroneopterin phosphate aldolase.
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7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
additional information
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7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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?
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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?
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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?
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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?
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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?
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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?
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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?
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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?
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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?
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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additional information
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the enzyme does not exhibit significant dihydroneopterin aldolase activity
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additional information
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the enzyme does not exhibit significant dihydroneopterin aldolase activity
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additional information
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the enzyme does not exhibit significant dihydroneopterin aldolase activity
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additional information
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the enzyme does not exhibit significant dihydroneopterin aldolase activity
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additional information
?
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the enzyme does not exhibit significant dihydroneopterin aldolase activity
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additional information
?
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the enzyme does not exhibit significant dihydroneopterin aldolase activity
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?
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7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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?
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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?
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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?
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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-
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?
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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?
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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?
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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?
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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?
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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?
7,8-dihydroneopterin 3'-triphosphate
6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Uniprot
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UniProt
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UniProt
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no activity in Haloferax volcanii
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Q8F2M2_LEPIN
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
136
0
15962
TrEMBL
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FOLB1_ARATH
146
0
16281
Swiss-Prot
other Location (Reliability: 2 )
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sitting drop vapor diffusion method, using 0.1 M Tris hydrochloride (pH 7.2), 21% (w/v) polyethylene glycol 2000 MME, and 115 mM cyclohexylbutanoyl-N-hydroxyethylglucamide
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Q-Sepharose column chromatography and Superdex 200 gel filtration
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expressed in Escherichia coli DH5alpha cells
expressed in Escherichia coli M15 [pREP4] cells
expressed in Escherichia coli DH5alpha cells
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expressed in Escherichia coli DH5alpha cells
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expressed in Escherichia coli DH5alpha cells
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expressed in Escherichia coli DH5alpha cells
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expressed in Escherichia coli DH5alpha cells
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Phillips, G.; Grochowski, L.L.; Bonnett, S.; Xu, H.; Bailly, M.; Blaby-Haas, C.; El Yacoubi, B.; Iwata-Reuyl, D.; White, R.H.; de Crecy-Lagard, V.
Functional promiscuity of the COG0720 family
ACS Chem. Biol.
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197-209
2012
Clostridium botulinum, Clostridium botulinum 19397, Leptospira interrogans serovar Lai (Q8F2M2), Leptospira interrogans serovar Lai 56601 (Q8F2M2), no activity in Haloferax volcanii
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Pribat, A.; Jeanguenin, L.; Lara-Nunez, A.; Ziemak, M.J.; Hyde, J.E.; de Crecy-Lagard, V.; Hanson, A.D.
6-pyruvoyltetrahydropterin synthase paralogs replace the folate synthesis enzyme dihydroneopterin aldolase in diverse bacteria
J. Bacteriol.
191
4158-4165
2009
Clostridium botulinum, Leptospira interrogans, Leptospira interrogans L1-130, Plasmodium falciparum, Syntrophus aciditrophicus, Thermotoga maritima
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Bauer, S.; Schott, A.K.; Illarionova, V.; Bacher, A.; Huber, R.; Fischer, M.
Biosynthesis of tetrahydrofolate in plants crystal structure of 7,8-dihydroneopterin aldolase from Arabidopsis thaliana reveals a novel adolase class
J. Mol. Biol.
339
967-979
2004
Arabidopsis thaliana (Q9SF23)
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Dittrich, S.; Mitchell, S.; Blagborough, A.; Wang, Q.; Wang, P.; Sims, P.; Hyde, J.
An atypical orthologue of 6-pyruvoyltetrahydropterin synthase can provide the missing link in the folate biosynthesis pathway of malaria parasites
Mol. Microbiol.
67
609-618
2008
Plasmodium falciparum
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Hyde, J.; Dittrich, S.; Wang, P.; Sims, P.; de Crecy-Lagard, V.; Hanson, A.
Plasmodium falciparum a paradigm for alternative folate biosynthesis in diverse microorganisms?
Trends Parasitol.
24
502-508
2008
Plasmodium falciparum
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