Structural highlights
Function
RSAMH_PYRHO Catalyzes the hydrolysis of S-adenosyl-L-methionine (SAM) into adenosine and L-methionine (PubMed:18551689). Is likely stereoselective, specifically hydrolyzing (R)-S-adenosyl-L-methionine ((R)-SAM), the inactive form of the ubiquitous cofactor SAM, and not the active form of SAM, (S)-S-adenosyl-L-methionine (By similarity). Probaly plays a role in preventing accumulation of (R)-S-adenosyl-L-methionine in cells; maintenance of (S)-S-denosyl-L-methionine homochirality is important for cellular health given that the (R)-form is largely inactive as a methyl donor and can function as an inhibitor of methyltransferases (By similarity). Is unable to mediate a fluorination or chlorination reaction with SAM (PubMed:18551689).[UniProtKB:A4X4S2][1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Deng H, Botting CH, Hamilton JT, Russell RJ, O'Hagan D. S-adenosyl-L-methionine:hydroxide adenosyltransferase: a SAM enzyme. Angew Chem Int Ed Engl. 2008;47(29):5357-61. PMID:18551689 doi:10.1002/anie.200800794
