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EC Tree
IUBMB Comments Also acts on 5'-deoxyadenosine and other analogues having 5'-deoxy groups.
The taxonomic range for the selected organisms is: Pyrococcus furiosus The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
methylthioadenosine phosphorylase, 5'-methylthioadenosine phosphorylase, mta phosphorylase, mtap protein, 5'-deoxy-5'-methylthioadenosine phosphorylase, ssmtapii, ssmtap, mtapase, mesado phosphorylase, pfmtap,
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5'-deoxy-5'-methylthioadenosine phosphorylase
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5'-deoxy-5'-methylthioadenosine phosphorylase
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5'-methylthioadenosine nucleosidase
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5'-methylthioadenosine phosphorylase
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MeSAdo phosphorylase
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MeSAdo/Ado phosphorylase
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methylthioadenosine nucleoside phosphorylase
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methylthioadenosine phosphorylase
MTA phosphorylase
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phosphorylase, methylthioadenosine
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methylthioadenosine phosphorylase
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methylthioadenosine phosphorylase
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pentosyl group transfer
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S-methyl-5'-thioadenosine:phosphate S-methyl-5-thio-alpha-D-ribosyl-transferase
Also acts on 5'-deoxyadenosine and other analogues having 5'-deoxy groups.
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5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
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adenosine + phosphate
adenine + D-ribose 1-phosphate
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guanosine + phosphate
guanine + D-ribose 1-phosphate
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inosine + phosphate
hypoxanthine + D-ribose 1-phosphate
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additional information
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additional information
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PfMTAP is characterized by a broad substrate specificity towards purine nucleosides, with a 20fold higher catalytic efficacy for adenosine and 5'-methylthioadenosine than for inosine and guanosine
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additional information
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PfMTAP is characterized by a broad substrate specificity towards purine nucleosides, with a 20fold higher catalytic efficacy for adenosine and 5'-methylthioadenosine than for inosine and guanosine
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additional information
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6-amino purine nucleosides are the preferred substrates, substrate specificity
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dithiothreitol
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0.8 M, reduction of thermostability
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0.147
5'-methylthioadenosine
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24.5
5'-methylthioadenosine
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86 - 95
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2 different activation energy-dependent processes occur below and above 100°C
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SwissProt
brenda
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30000
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6 * 30000, SDS-PAGE
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hexamer
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6 * 30000, SDS-PAGE
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100
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5 h, 98% remaining activity
137
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melting temperature
139
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melting temperature in presence of 100 mM phosphate
additional information
PfMTAP is a highly thermostable protein
additional information
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PfMTAP is a highly thermostable protein
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dithiothreitol 0.8 M, reduction of thermostability
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enzyme is extremely stable to proteolytic cleavage
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transition midpoint for guanidinium chloride-induced unfolding is 3.0 M after 22 h incubation. The value decreases to 2.0 M in presence of 30 mM dithiothreitol. The guanidinium chloride-induced unfolding is completely reversible
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1-propanol
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at 50%: 88% remaining activity after 60 min at 50°C, 58% remaining activity after 60 min at 70°C, 22% remaining activity after 60 min at 90°C
acetonitrile
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at 50%: stable at 90°C for 30 min, loss of 62% activity after 60 min
dimethylformamide
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at 50%: 48% remaining activity after 60 min at 50°C, 5% remaining activity after 60 min at 70°C, no activity at 90°C
Ethanol
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at 50%: 90% remaining activity after 60 min at 50°C, 65% remaining activity after 60 min at 70°C, 30% remaining activity after 60 min at 90°C
Methanol
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at 50%: stable at 90°C for 30 min, loss of 77% activity after 60 min
tetrahydrofuran
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at 50%: 77% remaining activity after 60 min at 50°C, 50% remaining activity after 60 min at 70°C, 3% remaining activity after 60 min at 90°C
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20°C, Tris-HCl 10 mM, pH 7.4, purified enzyme, stable for at least 1 year
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expressed in Escherichia coli
expression in Escherichia coli
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guanidinium chloride-induced unfolding is completely reversible
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Cacciapuoti, G.; Bertoldo, C.; Brio, A.; Zappia, V.; Porcelli, M.
Purification and characterization of 5'-methylthioadenosine phosphorylase from the hyperthermophilic archaeon Pyrococcus furiosus. Substrate specificity and primary structure analysis
Extremophiles
7
159-168
2003
Pyrococcus furiosus
brenda
Cacciapuoti, G.; Moretti, M.A.; Forte, S.; Brio, A.; Camardella, L.; Zappia, V.; Porcelli, M.
Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and assignment of disulfide bonds
Eur. J. Biochem.
271
4834-4844
2004
Pyrococcus furiosus
brenda
Cacciapuoti, G.; Marabotti, A.; Fuccio, F.; Porcelli, M.
Unraveling the structural and functional differences between purine nucleoside phosphorylase and 5-deoxy-5-methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus
Biochim. Biophys. Acta
1814
1358-1366
2011
Pyrococcus furiosus (Q8U4Q8), Pyrococcus furiosus
brenda