| formylmethanofuran-tetrahydromethanopterin N-formyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 formylmethanofuran-THMPT-formyltransferase tetramer, Methanopyrus kandleri | |||||||||
| Identifiers | |||||||||
| EC no. | 2.3.1.101 | ||||||||
| CAS no. | 105669-83-8 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
| FTR | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 formylmethanofuran:tetrahydromethanopterin fromyltransferase from methanosarcina barkeri | |||||||||
| Identifiers | |||||||||
| Symbol | FTR | ||||||||
| Pfam | PF01913 | ||||||||
| InterPro | IPR022667 | ||||||||
| SCOP2 | 1ftr / SCOPe / SUPFAM | ||||||||
| TCDB | 9.A.17 | ||||||||
| |||||||||
| FTR, proximal lobe | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 formylmethanofuran:tetrahydromethanopterin formyltransferase from archaeoglobus fulgidus | |||||||||
| Identifiers | |||||||||
| Symbol | FTR_C | ||||||||
| Pfam | PF02741 | ||||||||
| InterPro | IPR002770 | ||||||||
| SCOP2 | 1ftr / SCOPe / SUPFAM | ||||||||
| |||||||||
In enzymology, a formylmethanofuran-tetrahydromethanopterin N-formyltransferase (EC 2.3.1.101) is an enzyme that catalyzes the chemical reaction
Contents
- 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]
