S-methyl-5'-thioadenosine phosphorylase

S-methyl-5-thioadenosine phosphorylase
S-methyl-5'-thioadenosine phosphorylase trimer, Human
Identifiers
EC no.	2.4.2.28
CAS no.	61970-06-7
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
Search PMC articles PubMed articles NCBI proteins

In enzymology, a S-methyl-5'-thioadenosine phosphorylase (EC 2.4.2.28) is an enzyme that catalyzes the chemical reaction

S-methyl-5'-thioadenosine + phosphate ${\displaystyle \rightleftharpoons }$ adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate

Thus, the two substrates of this enzyme are S-methyl-5'-thioadenosine and phosphate, whereas its two products are adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate.

This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is S-methyl-5-thioadenosine:phosphate S-methyl-5-thio-alpha-D-ribosyl-transferase. Other names in common use include 5'-methylthioadenosine nucleosidase, 5'-deoxy-5'-methylthioadenosine phosphorylase, MTA phosphorylase, MeSAdo phosphorylase, MeSAdo/Ado phosphorylase, methylthioadenosine phosphorylase, methylthioadenosine nucleoside phosphorylase, 5'-methylthioadenosine:phosphate methylthio-D-ribosyl-transferase, and S-methyl-5-thioadenosine phosphorylase. This enzyme participates in methionine metabolism.

Structural studies

As of late 2007, 20 structures have been solved for this class of enzymes, with PDB accession codes 1CB0, 1CG6, 1JDS, 1JDT, 1JDU, 1JDV, 1JDZ, 1JE0, 1JE1, 1JP7, 1JPV, 1K27, 1ODI, 1ODJ, 1ODK, 1SD1, 1SD2, 1V4N, 1WTA, and 2A8Y.

References

• Gambacorta A, Zappia V (1979). "5'-Methylthioadenosine phosphorylase from Caldariella acidophila Purification and properties". Eur. J. Biochem. 101 (2): 317–24. doi:10.1111/j.1432-1033.1979.tb19723.x. PMID 118001.
• Garbers DL (1978). "Demonstration of 5'-methylthioadenosine phosphorylase activity in various rat tissues. Some properties of the enzyme from rat lung". Biochim. Biophys. Acta. 523 (1): 82–93. doi:10.1016/0005-2744(78)90011-6. PMID 415762.
• Pegg AE, Williams-Ashman HG (1969). "Phosphate-stimulated breakdown of 5'-methylthioadenosine by rat ventral prostate". Biochem. J. 115 (2): 241–7. doi:10.1042/bj1150241. PMC 1185095. PMID 5378381.