The Enzyme Database

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EC 3.5.4.16     
Accepted name: GTP cyclohydrolase I
Reaction: GTP + H2O = formate + 7,8-dihydroneopterin 3′-triphosphate
For diagram of the early stages of folate biosynthesis, click here
Glossary: 7,8-dihydroneopterin 3′-triphosphate = 6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterin
Other name(s): GTP cyclohydrolase; guanosine triphosphate cyclohydrolase; guanosine triphosphate 8-deformylase; dihydroneopterin triphosphate synthase; GTP 8-formylhydrolase
Systematic name: GTP 7,8-8,9-dihydrolase
Comments: The reaction involves hydrolysis of two C-N bonds and isomerization of the pentose unit; the recyclization may be non-enzymic. This enzyme is involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 (sepiapterin reductase) and EC 4.2.3.12 (6-pyruvoyltetrahydropterin synthase) [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-19-3
References:
1.  Burg, A.W. and Brown, G.M. The biosynthesis of folic acid. 8. Purification and properties of the enzyme that catalyzes the production of formate from carbon atom 8 of guanosine triphosphate. J. Biol. Chem. 243 (1968) 2349–2358. [PMID: 4296838]
2.  Wolf, W.A. and Brown, G.M. The biosynthesis of folic acid. X. Evidence for an Amadori rearrangement in the enzymatic formation of dihydroneopterin triphosphate from GTP. Biochim. Biophys. Acta 192 (1969) 468–478. [DOI] [PMID: 4904679]
3.  Supangat, S., Choi, Y.K., Park, Y.S., Son, D., Han, C.D. and Lee, K.H. Expression, purification, crystallization and preliminary X-ray analysis of sepiapterin reductase from Chlorobium tepidum. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (2005) 202–204. [DOI] [PMID: 16510994]
[EC 3.5.4.16 created 1972]
 
 
EC 3.6.1.67     
Accepted name: dihydroneopterin triphosphate diphosphatase
Reaction: 7,8-dihydroneopterin 3′-triphosphate + H2O = 7,8-dihydroneopterin 3′-phosphate + diphosphate
Other name(s): folQ (gene name); nudB (gene name); NUDT1 (gene name); dihydroneopterin triphosphate pyrophosphohydrolase
Systematic name: 7,8-dihydroneopterin 3′-triphosphate diphosphohydrolase
Comments: The enzyme participates in a folate biosynthesis pathway, which is found in bacteria, fungi, and plants. Requires Mg2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Suzuki, Y. and Brown, G.M. The biosynthesis of folic acid. XII. Purification and properties of dihydroneopterin triphosphate pyrophosphohydrolase. J. Biol. Chem. 249 (1974) 2405–2410. [PMID: 4362677]
2.  O'Handley, S.F., Frick, D.N., Bullions, L.C., Mildvan, A.S. and Bessman, M.J. Escherichia coli orf17 codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT family of proteins. Cloning, purification, and characterization of the enzyme. J. Biol. Chem. 271 (1996) 24649–24654. [DOI] [PMID: 8798731]
3.  Klaus, S.M., Wegkamp, A., Sybesma, W., Hugenholtz, J., Gregory, J.F., 3rd and Hanson, A.D. A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of bacteria and plants. J. Biol. Chem. 280 (2005) 5274–5280. [DOI] [PMID: 15611104]
4.  Gabelli, S.B., Bianchet, M.A., Xu, W., Dunn, C.A., Niu, Z.D., Amzel, L.M. and Bessman, M.J. Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis. Structure 15 (2007) 1014–1022. [DOI] [PMID: 17698004]
[EC 3.6.1.67 created 2014]
 
 
EC 4.1.2.50     
Accepted name: 6-carboxytetrahydropterin synthase
Reaction: 7,8-dihydroneopterin 3′-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + triphosphate
For diagram of queuine biosynthesis, click here
Glossary: 7,8-dihydroneopterin 3′-triphosphate = 2-amino-6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-4-oxo-2,3,7,8-tetrahydropteridine
6-carboxy-5,6,7,8-tetrahydropterin = 2-amino-4-oxo-2,3,5,6,7,8-hexahydropteridine-6-carboxylate
Other name(s): CPH4 synthase; queD (gene name); ToyB; ykvK (gene name)
Systematic name: 7,8-dihydroneopterin 3′-triphosphate acetaldehyde-lyase (6-carboxy-5,6,7,8-tetrahydropterin and triphosphate-forming)
Comments: Binds Zn2+. Isolated from the bacteria Bacillus subtilis and Escherichia coli. The reaction is part of the biosynthesis pathway of queuosine.The enzyme from Escherichia coli can also convert 6-pyruvoyl-5,6,7,8-tetrahydropterin and sepiapterin to 6-carboxy-5,6,7,8-tetrahydropterin [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Cicmil, N. and Shi, L. Crystallization and preliminary X-ray characterization of queD from Bacillus subtilis, an enzyme involved in queuosine biosynthesis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 119–122. [DOI] [PMID: 18259064]
2.  McCarty, R.M., Somogyi, A. and Bandarian, V. Escherichia coli QueD is a 6-carboxy-5,6,7,8-tetrahydropterin synthase. Biochemistry 48 (2009) 2301–2303. [DOI] [PMID: 19231875]
[EC 4.1.2.50 created 2012]
 
 
EC 4.1.2.60     
Accepted name: dihydroneopterin triphosphate aldolase
Reaction: 7,8-dihydroneopterin 3′-triphosphate = 6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate
Other name(s): PTPS-III
Systematic name: 7,8-dihydroneopterin 3′-triphosphate glycolaldehyde phosphate-lyase [6-(hydroxymethyl)-7,8-dihydropterin-forming]
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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Dittrich, S., Mitchell, S.L., Blagborough, A.M., Wang, Q., Wang, P., Sims, P.F. and Hyde, J.E. An atypical orthologue of 6-pyruvoyltetrahydropterin synthase can provide the missing link in the folate biosynthesis pathway of malaria parasites. Mol. Microbiol. 67 (2008) 609–618. [DOI] [PMID: 18093090]
2.  Hyde, J.E., Dittrich, S., Wang, P., Sims, P.F., de Crecy-Lagard, V. and Hanson, A.D. Plasmodium falciparum: a paradigm for alternative folate biosynthesis in diverse microorganisms. Trends Parasitol. 24 (2008) 502–508. [DOI] [PMID: 18805734]
3.  Pribat, A., Jeanguenin, L., Lara-Nunez, A., Ziemak, M.J., Hyde, J.E., de Crecy-Lagard, V. and Hanson, A.D. 6-pyruvoyltetrahydropterin synthase paralogs replace the folate synthesis enzyme dihydroneopterin aldolase in diverse bacteria. J. Bacteriol. 191 (2009) 4158–4165. [DOI] [PMID: 19395485]
[EC 4.1.2.60 created 2017]
 
 
EC 4.2.3.12     
Accepted name: 6-pyruvoyltetrahydropterin synthase
Reaction: 7,8-dihydroneopterin 3′-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
For diagram of biopterin biosynthesis, click here
Glossary: 7,8-dihydroneopterin 3′-triphosphate = 6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterin
Other name(s): 2-amino-4-oxo-6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydroxypteridine triphosphate lyase; 6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterin triphosphate-lyase (6-pyruvoyl-5,6,7,8-tetrahydropterin-forming)
Systematic name: 7,8-dihydroneopterin 3′-triphosphate triphosphate-lyase (6-pyruvoyl-5,6,7,8-tetrahydropterin-forming)
Comments: Catalyses triphosphate elimination and an intramolecular redox reaction in the presence of Mg2+. It has been identified in human liver. This enzyme is involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 (sepiapterin reductase) and EC 3.5.4.16 (GTP cyclohydrolase I) [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 97089-82-2
References:
1.  Milstien, S., Kaufman, S. The biosynthesis of tetrahydrobiopterin in rat brain. Purification and characterization of 6-pyruvoyl-tetrahydrobiopterin(2′-oxo) reductase. J. Biol. Chem. 264 (1989) 8066–8073. [PMID: 2656673]
2.  Thöny, B., Leimbacher, W., Bürgisser, D., Heinzmann, C.W. Human 6-pyruvoyl-tetrahydrobiopterin synthase: cDNA cloning and heterologous expression of the recombinant enzyme. Biochem. Biophys. Res. Commun. 189 (1992) 1437–1443. [DOI] [PMID: 1282802]
3.  Supangat, S., Choi, Y.K., Park, Y.S., Son, D., Han, C.D. and Lee, K.H. Expression, purification, crystallization and preliminary X-ray analysis of sepiapterin reductase from Chlorobium tepidum. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (2005) 202–204. [DOI] [PMID: 16510994]
[EC 4.2.3.12 created 1999 as EC 4.6.1.10, transferred 2000 to EC 4.2.3.12, modified 2001]
 
 
EC 5.1.99.7     
Accepted name: dihydroneopterin triphosphate 2′-epimerase
Reaction: 7,8-dihydroneopterin 3′-triphosphate = 7,8-dihydromonapterin 3′-triphosphate
For diagram of monapterin biosynthesis, click here
Glossary: 7,8-dihydroneopterin 3′-triphosphate = (2R,3S)-3-(2-amino-4-oxo-3,4,7,8-tetrahydropteridin-6-yl)-2,3-dihydroxypropyl triphosphate
7,8-dihydromonapterin 3′-triphosphate = (2S,3S)-3-(2-amino-4-oxo-3,4,7,8-tetrahydropteridin-6-yl)-2,3-dihydroxypropyl triphosphate
Other name(s): D-erythro-7,8-dihydroneopterin triphosphate epimerase; folX (gene name)
Systematic name: 7,8-dihydroneopterin 3′-triphosphate 2′-epimerase
Comments: The enzyme, found in gammaproteobacteria, has almost no activity with 7,8-dihydroneopterin [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ahn, C., Byun, J. and Yim, J. Purification, cloning, and functional expression of dihydroneopterin triphosphate 2′-epimerase from Escherichia coli. J. Biol. Chem. 272 (1997) 15323–15328. [DOI] [PMID: 9182560]
2.  Haussmann, C., Rohdich, F., Schmidt, E., Bacher, A. and Richter, G. Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase. J. Biol. Chem. 273 (1998) 17418–17424. [DOI] [PMID: 9651328]
[EC 5.1.99.7 created 2015]
 
 


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