2003
DOI: 10.1007/s00792-002-0307-2
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Purification and characterization of 5′-methylthioadenosine phosphorylase from the hyperthermophilic archaeon Pyrococcus furiosus

Abstract: 5'-Methylthioadenosine phosphorylase (MTAP) was purified to homogeneity from the hyperthermophilic archaeon Pyrococcus furiosus. The protein is a homoexamer of 180 kDa. The enzyme is highly thermoactive, with an optimum temperature of 125 degrees C, and extremely thermostable, retaining 98% residual activity after 5 h at 100 degrees C and showing a half-life of 43 min at 130 degrees C. In the presence of 100 mM phosphate, the apparent T(m) (137 degrees C) increases to 139 degrees C. The enzyme is extremely sta… Show more

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Cited by 34 publications
(45 citation statements)
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“…The structural gene of PfMTAP encodes a protein of 257 residues with a predicted molecular mass of 29 219 Da, which is in good agreement with that of 30 ± 1 kDa estimated by biochemical analyses for the native enzyme [21].…”
Section: Resultssupporting
confidence: 75%
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“…The structural gene of PfMTAP encodes a protein of 257 residues with a predicted molecular mass of 29 219 Da, which is in good agreement with that of 30 ± 1 kDa estimated by biochemical analyses for the native enzyme [21].…”
Section: Resultssupporting
confidence: 75%
“…IPTG-induced E. coli cells transformed with pET-MTAP produced 1.77 mg of recombinant protein per gram of cells: thus the expression is about 15-fold higher than for MTAP from P. furiosus [21].…”
Section: Resultsmentioning
confidence: 93%
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