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Literature summary extracted from

  • Cacciapuoti, G.; Fusco, S.; Caiazzo, N.; Zappia, V.; Porcelli, M.
    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 (1999), Protein Expr. Purif., 16, 125-135.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.2.28 expression at a high level in Escherichia coli Saccharolobus solfataricus
2.4.2.28 overexpression in Escherichia coli strain RB791, amino acid determination, incorrect positioning of disulfide bonds, the recombinant enzyme is less thermostable and thermophilic than the native enzyme Saccharolobus solfataricus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.28 guanidine hydrochloride only recombinant enzyme Saccharolobus solfataricus
2.4.2.28 iodoacetamide only recombinant enzyme Saccharolobus solfataricus
2.4.2.28 iodoacetate only recombinant enzyme Saccharolobus solfataricus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.2.28 0.024
-
5'-methylthioadenosine recombinant enzyme Saccharolobus solfataricus
2.4.2.28 0.024
-
5'-methylthioadenosine wild-type and recombinant enzyme Saccharolobus solfataricus
2.4.2.28 0.125
-
phosphate recombinant enzyme Saccharolobus solfataricus
2.4.2.28 0.125
-
phosphate wild-type and recombinant enzyme Saccharolobus solfataricus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.2.28 27000
-
6 * 27000, recombinant enzyme, SDS-PAGE Saccharolobus solfataricus
2.4.2.28 160000
-
gel filtration Saccharolobus solfataricus
2.4.2.28 160000
-
recombinant enzyme, gel filtration Saccharolobus solfataricus
2.4.2.28 160000
-
recombinant enzyme Saccharolobus solfataricus

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.28 Saccharolobus solfataricus
-
-
-
2.4.2.28 Saccharolobus solfataricus P50389
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.2.28 recombinant enzyme Saccharolobus solfataricus
2.4.2.28 recombinant from Escherichia coli Saccharolobus solfataricus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.2.28 2.115
-
-
Saccharolobus solfataricus
2.4.2.28 2.12
-
purified recombinant enzyme Saccharolobus solfataricus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.28 5'-methylthioadenosine + phosphate
-
Saccharolobus solfataricus adenine + 5-methylthio-D-ribose 1-phosphate
-
?

Subunits

EC Number Subunits Comment Organism
2.4.2.28 hexamer 6 * 27000, recombinant enzyme, SDS-PAGE Saccharolobus solfataricus

Synonyms

EC Number Synonyms Comment Organism
2.4.2.28 5'-methylthioadenosine phosphorylase
-
Saccharolobus solfataricus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.2.28 70
-
assay at Saccharolobus solfataricus
2.4.2.28 100
-
recombinant enzyme Saccharolobus solfataricus
2.4.2.28 120
-
wild-type enzyme Saccharolobus solfataricus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.4.2.28 30 120 recombinant enzyme Saccharolobus solfataricus
2.4.2.28 60 120 60°C: about 40% of maximal activity, 120°C: about 40% of maximal activity, recombinant enzyme Saccharolobus solfataricus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.4.2.28 additional information
-
the recombinant enzyme, expressed in Escherichia coli, is less thermostable and thermophilic than the native enzyme due to incorrect positioning of disulfide bonds Saccharolobus solfataricus
2.4.2.28 additional information
-
the recombinant 5'-methylthioadenosine phosphorylase is less thermophilic and thermostable than the Sulfolobus solfataricus enzyme, since an incorrect positioning of disulfide bonds within the molecule generates structures less stable to thermal unfolding Saccharolobus solfataricus
2.4.2.28 70
-
recombinant enzyme, 0.8 M DTT, stable Saccharolobus solfataricus
2.4.2.28 90
-
recombinant enzyme, 0.8 M DTT, 2 h, loss of 38% activity Saccharolobus solfataricus
2.4.2.28 100
-
recombinant enzyme, 1 h, 85% remaining activity Saccharolobus solfataricus
2.4.2.28 100
-
1 h, 15% loss of activity of recombinant enzyme, wild-type enzyme remains stable Saccharolobus solfataricus
2.4.2.28 111
-
recombinant enzyme, melting temperature Saccharolobus solfataricus
2.4.2.28 111
-
melting temperature of recombinant enzyme Saccharolobus solfataricus
2.4.2.28 118
-
recombinant enzyme in presence of 100 mM phosphate, melting temperature Saccharolobus solfataricus