PMID: 118001Nov 1, 1979Paper

5'-Methylthioadenosine phosphorylase from Caldariella acidophila. Purification and properties

European Journal of Biochemistry
M Carteni'-FarinaV Zappia

Abstract

The occurrence of 5'-methylthioadenosine phosphorylase in Caldariella acidophila, a thermophilic bacterium growing optimally at 87 degrees C, is reported. It represents the first example in prokaryotes of a phosphoryolytic cleavage of the thioether. The reaction products, purified by ion-exchange chromatography, have been identified as 5-methylthioribose-1-phosphate and adenine by several analytical procedures. The enzyme has been purified to homogeneity in 32% yield by using DEAE-cellulose and hydroxyapatite chromatography, gel filtration and isoelectric focusing. The enzyme shows a high degree of thermophilicity, its temperature optimum being at 93 degrees C; furthermore no loss of activity is observable after exposure for 1 h at 100 degrees C. The kinetic data indicate a sequential mechanism of the reaction. The apparent Km values are 0.095 mM for 5'-methylthioadenosine and 6.1 mM for phosphate. The specificity of the reaction is rather strict. Experiments performed with analogues of the substrate, i.e. 5'-methylthioinosine, 5'-dimethylthioadenosine sulfonium salt, 5'-n-butylthioadenosine, 5'-isobutylthioadenosine, 5'-isobutylthioinosine, adenosylhomocysteine, 5'-thioethanoladenosine, adenosine, indicate the relevance of the...Continue Reading

References

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Citations

Oct 24, 2007·Antimicrobial Agents and Chemotherapy·Janice R SufrinC J Bacchi
Jan 29, 2016·Molecular & Cellular Proteomics : MCP·Emilie Bigaud, Fernando J Corrales
Oct 12, 2018·Microbial Biotechnology·Agnieszka SekowskaAntoine Danchin

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