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- Name help_outline 5,10-methylenetetrahydrosulfopterin Identifier CHEBI:140606 Charge 0 Formula C19H26N6O5 InChIKeyhelp_outline ANKAHQUVZAJBJB-HUORLRHWSA-N SMILEShelp_outline N12C3=C(NCC1CN(C4=CC=C(C=C4)C[C@@H]([C@@H]([C@@H](CO)O)O)O)C2)N=C(NC3=O)N 2D coordinates Mol file for the small molecule Search links Involved in 1 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 142 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 6,204 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 78 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline tetrahydrosulfopterin Identifier CHEBI:140605 Charge 0 Formula C18H26N6O5 InChIKeyhelp_outline NAKPFGZQINPHPR-FLTXBFBQSA-N SMILEShelp_outline C=12C(NC(=NC1NCC(N2)CNC3=CC=C(C=C3)C[C@@H]([C@@H]([C@@H](CO)O)O)O)N)=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:56608 | RHEA:56609 | RHEA:56610 | RHEA:56611 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Purification and properties of serine hydroxymethyltransferase from Sulfolobus solfataricus.
Delle Fratte S., White R.H., Maras B., Bossa F., Schirch V.
Serine hydroxymethyltransferase (SHMT) catalyzes the reversible cleavage of serine to glycine with the transfer of the one-carbon group to tetrahydrofolate to form 5,10-methylenetetrahydrofolate. No SHMT has been purified from a nonmethanogenic Archaea strain, in part because this group of organis ... >> More
Serine hydroxymethyltransferase (SHMT) catalyzes the reversible cleavage of serine to glycine with the transfer of the one-carbon group to tetrahydrofolate to form 5,10-methylenetetrahydrofolate. No SHMT has been purified from a nonmethanogenic Archaea strain, in part because this group of organisms uses modified folates as the one-carbon acceptor. These modified folates are not readily available for use in assays for SHMT activity. This report describes the purification and characterization of SHMT from the thermophilic organism Sulfolobus solfataricus. The exchange of the alpha-proton of glycine with solvent protons in the absence of the modified folate was used as the activity assay. The purified protein catalyzes the synthesis of serine from glycine and a synthetic derivative of a fragment of the natural modified folate found in S. solfataricus. Replacement of the modified folate with tetrahydrofolate did not support serine synthesis. In addition, this SHMT also catalyzed the cleavage of both allo-threonine and beta-phenylserine in the absence of the modified folate. The cleavage of these two amino acids in the absence of tetrahydrofolate is a property of other characterized SHMTs. The enzyme contains covalently bound pyridoxal phosphate. Sequences of three peptides showed significant similarity with those of peptides of SHMTs from two methanogens. << Less