5,10-methylenetetrahydromethanopterin reductase

In enzymology, a 5,10-methylenetetrahydromethanopterin reductase (EC 1.5.99.11) is an enzyme that catalyzes the chemical reaction

5-methyltetrahydromethanopterin + coenzyme F420 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420
coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase
Identifiers
EC number1.5.99.11
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Thus, the two substrates of this enzyme are 5-methyltetrahydromethanopterin and coenzyme F420, whereas its two products are 5,10-methylenetetrahydromethanopterin 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-methyltetrahydromethanopterin:coenzyme-F420 oxidoreductase. Other names in common use include 5,10-methylenetetrahydromethanopterin cyclohydrolase, N5,N10-methylenetetrahydromethanopterin reductase, methylene-H4MPT reductase, coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin, reductase, and N5,N10-methylenetetrahydromethanopterin:coenzyme-F420 oxidoreductase. This enzyme participates in folate biosynthesis.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1Z69.

References

    • Ma K, Thauer RK (1990). "Purification and properties of N5, N10-methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum (strain Marburg)". Eur. J. Biochem. 191 (1): 187–93. doi:10.1111/j.1432-1033.1990.tb19109.x. PMID 2379499.
    • 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.
    • Ma K, Thauer RK (1990). "Single step purification of methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum by specific binding to blue sepharose CL-6B". FEBS Lett. 268 (1): 59–62. doi:10.1016/0014-5793(90)80972-L. PMID 1696553. S2CID 26822476.
    • Vogels GD; Hensgens, CM; Keltjens, JT; Van Der Drift, C; Vogels, GD (1990). "Purification and properties of 5,10-methylenetetrahydromethanopterin reductase, a coenzyme F420-dependent enzyme, from Methanobacterium thermoautotrophicum strain delta H". J. Biol. Chem. 265 (4): 1852–7. PMID 2298726.
    • Drift C, Vogels GD (1990). "Purification and properties of 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanosarcina barkeri". J. Bacteriol. 172 (2): 564–71. doi:10.1128/jb.172.2.564-571.1990. PMC 208478. PMID 2298699.
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