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Heterologous expression of 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus: characterization of the recombinant protein and involvement of disulfide bonds in thermophilicity and thermostability.
Protein Expr Purif. 1999 Jun;16(1):125-35. doi: 10.1006/prep.1999.1076.
Protein Expr Purif. 1999.
PMID: 10336870
Three-dimensional structure of a hyperthermophilic 5'-deoxy-5'-methylthioadenosine phosphorylase from Sulfolobus solfataricus.
Appleby TC, Mathews II, Porcelli M, Cacciapuoti G, Ealick SE.
Appleby TC, et al.
J Biol Chem. 2001 Oct 19;276(42):39232-42. doi: 10.1074/jbc.M105694200. Epub 2001 Aug 6.
J Biol Chem. 2001.
PMID: 11489901
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Purification and characterization of extremely thermophilic and thermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Purine nucleoside phosphorylase activity and evidence for intersubunit disulfide bonds.
Cacciapuoti G, Porcelli M, Bertoldo C, De Rosa M, Zappia V.
Cacciapuoti G, et al.
J Biol Chem. 1994 Oct 7;269(40):24762-9.
J Biol Chem. 1994.
PMID: 7929153
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Extremely thermophilic and thermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Gene cloning and amino acid sequence determination.
Cacciapuoti G, Porcelli M, Bertoldo C, Fusco S, De Rosa M, Zappia V.
Cacciapuoti G, et al.
Eur J Biochem. 1996 Aug 1;239(3):632-7. doi: 10.1111/j.1432-1033.1996.0632u.x.
Eur J Biochem. 1996.
PMID: 8774706
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