The Enzyme Database

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EC 2.4.2.28     
Accepted name: S-methyl-5′-thioadenosine phosphorylase
Reaction: S-methyl-5′-thioadenosine + phosphate = adenine + S-methyl-5-thio-α-D-ribose 1-phosphate
For diagram of the methionine-salvage pathway, click here
Other name(s): 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; S-methyl-5-thioadenosine phosphorylase; S-methyl-5-thioadenosine:phosphate S-methyl-5-thio-α-D-ribosyl-transferase
Systematic name: S-methyl-5′-thioadenosine:phosphate S-methyl-5-thio-α-D-ribosyl-transferase
Comments: Also acts on 5′-deoxyadenosine and other analogues having 5′-deoxy groups.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 61970-06-7
References:
1.  Carteni-Farina, M., Oliva, A., Romeo, G., Napolitano, G., De Rosa, M., Gambacorta, A. and Zappia, V. 5′-Methylthioadenosine phosphorylase from Caldariella acidophila. Purification and properties. Eur. J. Biochem. 101 (1979) 317–324. [PMID: 118001]
2.  Garbers, D.L. Demonstration of 5′-methylthioadenosine phosphorylase activity in various rat tissues. Some properties of the enzyme from rat lung. Biochim. Biophys. Acta 523 (1978) 82–93. [PMID: 415762]
3.  Pegg, A.E. and Williams-Ashman, H.G. Phosphate-stimulated breakdown of 5′-methylthioadenosine by rat ventral prostate. Biochem. J. 115 (1969) 241–247. [PMID: 5378381]
[EC 2.4.2.28 created 1983]
 
 


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