1. Structural studies

2. References

3. Further reading

In enzymology, a formylmethanofuran-tetrahydromethanopterin N-formyltransferase ({{EC number|2.3.1.101}}) is an enzyme that catalyzes the chemical reaction

formylmethanofuran + 5,6,7,8-tetrahydromethanopterin methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin

Thus, the two substrates of this enzyme are formylmethanofuran and 5,6,7,8-tetrahydromethanopterin, whereas its two products are methanofuran and 5-formyl-5,6,7,8-tetrahydromethanopterin.

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is formylmethanofuran:5,6,7,8-tetrahydromethanopterin 5-formyltransferase. Other names in common use include formylmethanofuran-tetrahydromethanopterin formyltransferase, formylmethanofuran:tetrahydromethanopterin formyltransferase, N-formylmethanofuran(CHO-MFR):tetrahydromethanopterin(H4MPT), formyltransferase, FTR, formylmethanofuran:5,6,7,8-tetrahydromethanopterin, and N5-formyltransferase. This enzyme participates in folate biosynthesis.

Ftr from the thermophilic methanogen Methanopyrus kandleri (which has an optimum growth temperature 98 degrees C) is a hyperthermophilic enzyme that is absolutely dependent on the presence of lyotropic salts for activity and thermostability. The crystal structure of Ftr, determined to a reveals a homotetramer composed essentially of two dimers. Each subunit is subdivided into two tightly associated lobes both consisting of a predominantly antiparallel beta sheet flanked by alpha helices forming an alpha/beta sandwich structure. The approximate location of the active site was detected in a region close to the dimer interface.^[1] Ftr from the mesophilic methanogen Methanosarcina barkeri and the sulphate-reducing archaeon Archaeoglobus fulgidus have a similar structure.^[2]

In the methylotrophic bacterium Methylobacterium extorquens, Ftr interacts with three other polypeptides to form an Ftr/hydrolase complex which catalyses the hydrolysis of formyl-tetrahydromethanopterin to formate during growth on C1 substrates.^[3]

Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1FTR}}, {{PDB link|1M5H}}, {{PDB link|1M5S}}, {{PDB link|2FHJ}}, and {{PDB link|2FHK}}.

References

Further reading

• {{cite journal |vauthors=Donnelly MI, Wolfe RS | year = 1986 | title = The role of formylmethanofuran: tetrahydromethanopterin formyltransferase in methanogenesis from carbon dioxide | journal = J. Biol. Chem. | volume = 261 | pages = 16653–9 | pmid = 3097011 | issue = 35 }}
• {{cite journal |vauthors=Leigh JA, Rinehart KL, Wolfe RS | year = 1984 | title = Structure of methanofuran, the carbon-dioxide reduction factor of Methanobacterium thermoautotrophicum | journal = J. Am. Chem. Soc. | volume = 106 | pages = 3636–3640 | doi = 10.1021/ja00324a037 }}

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