formylmethanofuran-THMPT-formyltransferase tetramer, Methanopyrus kandleri
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / QuickGO|
formylmethanofuran:tetrahydromethanopterin fromyltransferase from methanosarcina barkeri
|SCOPe||1ftr / SUPFAM|
|FTR, proximal lobe|
formylmethanofuran:tetrahydromethanopterin formyltransferase from archaeoglobus fulgidus
|SCOPe||1ftr / SUPFAM|
- formylmethanofuran + 5,6,7,8-tetrahydromethanopterin methanofuran + 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. Ftr from the mesophilic methanogen Methanosarcina barkeri and the sulphate-reducing archaeon Archaeoglobus fulgidus have a similar structure.
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.
- Ermler U, Merckel M, Thauer R, Shima S (May 1997). "Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri - new insights into salt-dependence and thermostability". Structure. 5 (5): 635–46. doi:10.1016/s0969-2126(97)00219-0. PMID 9195883.
- Mamat B, Roth A, Grimm C, Ermler U, Tziatzios C, Schubert D, Thauer RK, Shima S (September 2002). "Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship". Protein Sci. 11 (9): 2168–78. doi:10.1110/ps.0211002. PMC 2373594. PMID 12192072.
- Pomper BK, Saurel O, Milon A, Vorholt JA (July 2002). "Generation of formate by the formyltransferase/hydrolase complex (Fhc) from Methylobacterium extorquens AM1". FEBS Lett. 523 (1–3): 133–7. doi:10.1016/S0014-5793(02)02962-9. PMID 12123819.
- Donnelly MI, Wolfe RS (1986). "The role of formylmethanofuran: tetrahydromethanopterin formyltransferase in methanogenesis from carbon dioxide". J. Biol. Chem. 261 (35): 16653–9. PMID 3097011.
- Leigh JA, Rinehart KL, Wolfe RS (1984). "Structure of methanofuran, the carbon-dioxide reduction factor of Methanobacterium thermoautotrophicum". J. Am. Chem. Soc. 106: 3636–3640. doi:10.1021/ja00324a037.
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