Methylenetetrahydromethanopterin dehydrogenase

methylenetetrahydromethanopterin dehydrogenase
Identifiers
EC number	1.5.98.1
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
Search PMC articles PubMed articles NCBI proteins

In enzymology, a methylenetetrahydromethanopterin dehydrogenase (EC 1.5.98.1) is an enzyme that catalyzes the chemical reaction

5,10-methylenetetrahydromethanopterin + coenzyme F₄₂₀ $\rightleftharpoons$ 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.