Enzymes
| UniProtKB help_outline | 146 proteins |
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- Name help_outline 5,10-methylenetetrahydromethanopterin Identifier CHEBI:57818 Charge -3 Formula C31H42N6O16P InChIKeyhelp_outline GBMIGEWJAPFSQI-CAFBYHECSA-K SMILEShelp_outline [H][C@]12[C@H](C)Nc3nc(N)[nH]c(=O)c3N1CN([C@@H]2C)c1ccc(C[C@H](O)[C@H](O)[C@H](O)CO[C@H]2O[C@H](COP([O-])(=O)O[C@@H](CCC([O-])=O)C([O-])=O)[C@@H](O)[C@H]2O)cc1 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline glycine Identifier CHEBI:57305 Charge 0 Formula C2H5NO2 InChIKeyhelp_outline DHMQDGOQFOQNFH-UHFFFAOYSA-N SMILEShelp_outline [NH3+]CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 135 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 5,6,7,8-tetrahydromethanopterin Identifier CHEBI:58103 Charge -3 Formula C30H42N6O16P InChIKeyhelp_outline SCBIBGUJSMHIAI-LHIIQLEZSA-K SMILEShelp_outline [H][C@]1(Nc2c(N[C@H]1C)nc(N)[nH]c2=O)[C@@H](C)Nc1ccc(C[C@H](O)[C@H](O)[C@H](O)CO[C@H]2O[C@H](COP([O-])(=O)O[C@@H](CCC([O-])=O)C([O-])=O)[C@@H](O)[C@H]2O)cc1 2D coordinates Mol file for the small molecule Search links Involved in 9 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-serine Identifier CHEBI:33384 Charge 0 Formula C3H7NO3 InChIKeyhelp_outline MTCFGRXMJLQNBG-REOHCLBHSA-N SMILEShelp_outline [NH3+][C@@H](CO)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 76 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:47104 | RHEA:47105 | RHEA:47106 | RHEA:47107 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Catalytic and thermodynamic properties of tetrahydromethanopterin-dependent serine hydroxymethyltransferase from Methanococcus jannaschii.
Angelaccio S., Chiaraluce R., Consalvi V., Buchenau B., Giangiacomo L., Bossa F., Contestabile R.
The reaction catalyzed by serine hydroxymethyltransferase (SHMT), the transfer of Cbeta of serine to tetrahydropteroylglutamate, represents in Eucarya and Eubacteria a major source of one-carbon (C1) units for several essential biosynthetic processes. In many Archaea, C1 units are carried by modif ... >> More
The reaction catalyzed by serine hydroxymethyltransferase (SHMT), the transfer of Cbeta of serine to tetrahydropteroylglutamate, represents in Eucarya and Eubacteria a major source of one-carbon (C1) units for several essential biosynthetic processes. In many Archaea, C1 units are carried by modified pterin-containing compounds, which, although structurally related to tetrahydropteroylglutamate, play a distinct functional role. Tetrahydromethanopterin, and a few variants of this compound, are the modified folates of methanogenic and sulfate-reducing Archaea. Little information on SHMT from Archaea is available, and the metabolic role of the enzyme in these organisms is not clear. This contribution reports on the purification and characterization of recombinant SHMT from the hyperthermophilic methanogen Methanococcus jannaschii. The enzyme was characterized with respect to its catalytic, spectroscopic, and thermodynamic properties. Tetrahydromethanopterin was found to be the preferential pteridine substrate. Tetrahydropteroylglutamate could also take part in the hydroxymethyltransferase reaction, although with a much lower efficiency. The catalytic features of the enzyme with substrate analogues and in the absence of a pteridine substrate were also very similar to those of SHMT isolated from Eucarya or Eubacteria. On the other hand, the M. jannaschii enzyme showed increased thermoactivity and resistance to denaturating agents with respect to the enzyme purified from mesophilic sources. The results reported suggest that the active site structure and the mechanism of SHMT are conserved in the enzyme from M. jannaschii, which appear to differ only in its ability to bind and use a modified folate as substrate and increased thermal stability. << Less