Methylenetetrahydromethanopterin dehydrogenase
| methylenetetrahydromethanopterin dehydrogenase | |||||||
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| Identifiers | |||||||
| EC number | 1.5.99.9 | ||||||
| CAS number | 100357-01-5 | ||||||
| Databases | |||||||
| IntEnz | IntEnz view | ||||||
| BRENDA | BRENDA entry | ||||||
| ExPASy | NiceZyme view | ||||||
| KEGG | KEGG entry | ||||||
| MetaCyc | metabolic pathway | ||||||
| PRIAM | profile | ||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||
| Gene Ontology | AmiGO / EGO | ||||||
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In enzymology, a methylenetetrahydromethanopterin dehydrogenase (EC 1.5.99.9) is an enzyme that catalyzes the chemical reaction
- 5,10-methylenetetrahydromethanopterin + coenzyme F420
5,10-methenyltetrahydromethanopterin + reduced coenzyme F420
Thus, the two substrates of this enzyme are 5,10-methylenetetrahydromethanopterin and coenzyme F420, whereas its two products are 5,10-methenyltetrahydromethanopterin and reduced coenzyme F420.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is 5,10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase. Other names in common use include N5,N10-methylenetetrahydromethanopterin dehydrogenase, and 5,10-methylenetetrahydromethanopterin dehydrogenase. This enzyme participates in folate biosynthesis.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1QV9, 1U6I, 1U6J, and 1U6K.
References
- Hartzell PL, Zvilius G, Escalante-Semerena JC, Donnelly MI (1985). "Coenzyme F420 dependence of the methylenetetrahydromethanopterin dehydrogenase of Methanobacterium thermoautotrophicum". Biochem. Biophys. Res. Commun. 133 (3): 884–90. doi:10.1016/0006-291X(85)91218-5. PMID 4084309.
- GD; Geerts, WJ; Keltjens, JT; Van Der Drift, C; Vogels, GD (1991). "Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri". Biochim. Biophys. Acta. 1079 (3): 293–302. doi:10.1016/0167-4838(91)90072-8. PMID 1911853.