| EC |
1.5.1.50 |
| Accepted name: |
dihydromonapterin reductase |
| Reaction: |
5,6,7,8-tetrahydromonapterin + NADP+ = 7,8-dihydromonapterin + NADPH + H+ |
| Glossary: |
7,8-dihydromonapterin = 2-amino-6-[(1S,2S)-1,2,3-trihydroxypropyl]-7,8-dihydropteridin-4(3H)-one |
| Other name(s): |
FolM; H2-MPt reductase |
| Systematic name: |
5,6,7,8-tetrahydromonapterin:NADP+ oxidoreductase |
| Comments: |
The enzyme, found in many Gram negative bacteria, also slowly reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate (cf. EC 1.5.1.3, dihydrofolate reductase). The enzyme has no activity with NADH. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Pribat, A., Blaby, I.K., Lara-Nunez, A., Gregory, J.F., 3rd, de Crecy-Lagard, V. and Hanson, A.D. FolX and FolM are essential for tetrahydromonapterin synthesis in Escherichia coli and Pseudomonas aeruginosa. J. Bacteriol. 192 (2010) 475–482. [DOI] [PMID: 19897652] |
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| [EC 1.5.1.50 created 2015] |
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| 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, PDB |
| 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] |
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| [EC 5.1.99.7 created 2015] |
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| EC |
5.1.99.8 |
| Accepted name: |
7,8-dihydroneopterin epimerase |
| Reaction: |
7,8-dihydroneopterin = 7,8-dihydromonapterin |
| Glossary: |
7,8-dihydroneopterin = 2-amino-6-[(1S,2R)-1,2,3-trihydroxypropyl]-7,8-dihydropteridin-4(3H)-one
7,8-dihydromonapterin = 2-amino-6-[(1S,2S)-1,2,3-trihydroxypropyl]-7,8-dihydropteridin-4(3H)-one |
| Systematic name: |
7,8-dihydroneopterin 2′-epimerase |
| Comments: |
The enzyme, which has been characterized in bacteria and plants, also has the activity of EC 4.1.2.25, dihydroneopterin aldolase. The enzyme from the bacterium Mycobacterium tuberculosis has an additional oxygenase function (EC 1.13.11.81, 7,8-dihydroneopterin oxygenase) [4]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
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] |
| 2. |
Goyer, A., Illarionova, V., Roje, S., Fischer, M., Bacher, A. and Hanson, A.D. Folate biosynthesis in higher plants. cDNA cloning, heterologous expression, and characterization of dihydroneopterin aldolases. Plant Physiol. 135 (2004) 103–111. [DOI] [PMID: 15107504] |
| 3. |
Czekster, C.M. and Blanchard, J.S. One substrate, five products: reactions catalyzed by the dihydroneopterin aldolase from Mycobacterium tuberculosis. J. Am. Chem. Soc. 134 (2012) 19758–19771. [DOI] [PMID: 23150985] |
| 4. |
Blaszczyk, J., Lu, Z., Li, Y., Yan, H. and Ji, X. Crystallographic and molecular dynamics simulation analysis of Escherichia coli dihydroneopterin aldolase. Cell Biosci 4:52 (2014). [DOI] [PMID: 25264482] |
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| [EC 5.1.99.8 created 2015] |
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