Structural highlights
Function
[GLYA1_MYCTU] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Chaturvedi S, Bhakuni V. Unusual structural, functional, and stability properties of serine hydroxymethyltransferase from Mycobacterium tuberculosis. J Biol Chem. 2003 Oct 17;278(42):40793-805. Epub 2003 Aug 11. PMID:12913008 doi:http://dx.doi.org/10.1074/jbc.M306192200
