Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.2.28 extracted from

  • Bagarolo, M.L.; Porcelli, M.; Martino, E.; Feller, G.; Cacciapuoti, G.
    Multiple disulfide bridges modulate conformational stability and flexibility in hyperthermophilic archaeal purine nucleoside phosphorylase (2015), Biochim. Biophys. Acta, 1854, 1458-1465.
    View publication on PubMed
Search for more literature for 2.4.2.28

Protein Variants

Protein Variants Comment Organism
C259S/C261S mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 102°C. Specific activity is similar to the activity of the wild-type enzyme Saccharolobus solfataricus
C259S/C261S/C262S mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 91°C. Specific activity is similar to the activity of the wild-type enzyme Saccharolobus solfataricus
C259S/C261S/C262S/C200S/C205S mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 73°C. Specific activity is similar to the activity of the wild-type enzyme Saccharolobus solfataricus
C259S/C261S/C262S/C200S/C205S/C138S mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 78°C. Specific activity is similar to the activity of the wild-type enzyme Saccharolobus solfataricus
C259S/C261S/C262S/C200S/C205S/C138S/C164S mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 73°C. Specific activity is similar to the activity of the wild-type enzyme Saccharolobus solfataricus
C262S mutation significantly reduces the optimal temperature for the catalytic activity. Strong destabilization for the folded structure of the enzyme, as inferred from the temperature for half inactivation, which decreases from 112°C (wild-type) to 106°C. Specific activity is similar to the activity of the wild-type enzyme Saccharolobus solfataricus

General Stability

General Stability Organism
elimination of the disulfide bond Cys138–Cys205 leads to an increased protease susceptibility Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q97W94
-
-
Saccharolobus solfataricus P2 Q97W94
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.86
-
 70°C, pH 7.4, mutant enzyme C259S/C261S/C262S/C200S/C205S Saccharolobus solfataricus
4.97
-
 70°C, pH 7.4, mutant enzyme C262S Saccharolobus solfataricus
5.09
-
 70°C, pH 7.4, mutant enzyme C259S/C261S Saccharolobus solfataricus
5.28
-
 70°C, pH 7.4, mutant enzyme C259S/C261S/C262S/C200S/C205S/C138S/C164S Saccharolobus solfataricus
5.68
-
 70°C, pH 7.4, mutant enzyme C259S/C261S/C262S Saccharolobus solfataricus
6.24
-
 70°C, pH 7.4, mutant enzyme C259S/C261S/C262S/C200S/C205S/C138S Saccharolobus solfataricus
6.27
-
 70°C, pH 7.4, wild-type enzyme Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5'-deoxy-5'-methylthioadenosine + phosphate
-
 Saccharolobus solfataricus adenine + 5-methylthio-D-ribose 1-phosphate
-
 ?
5'-deoxy-5'-methylthioadenosine + phosphate
-
 Saccharolobus solfataricus P2 adenine + 5-methylthio-D-ribose 1-phosphate
-
 ?

Subunits

Subunits Comment Organism
hexamer
-
 Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
5'-deoxy-5'-methylthioadenosine phosphorylase II
-
 Saccharolobus solfataricus
SsMTAPII
-
 Saccharolobus solfataricus
SSO2343 locus name Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
107
-
 mutant enzyme C259S/C261S/C262S/C200S/C205S/C164S Saccharolobus solfataricus
112
-
 mutant enzyme C259S/C261S/C262S/C200S/C205S Saccharolobus solfataricus
114
-
 mutant enzyme C259S/C261S/C262S/C200S/C205S and mutant enzyme C259S/C261S/C262S Saccharolobus solfataricus
115
-
 mutant enzyme C259S/C261S and mutant enzyme C259S Saccharolobus solfataricus
120
-
 wild-type enzyme Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 the hexameric hyperthermophilic protein contains in each subunit two pairs of disulfide bridges, a CXC motif, and one free cysteine. All cysteine pairs and especially the CXC motif significantly contribute to the enzyme thermal stability Saccharolobus solfataricus
73
-
 5 min, 50% residual activity, mutant enzyme C259S/C261S/C262S/C200S/C205S and mutant enzyme C259S/C261S/C262S/C200S/C205S/C138S/C164S Saccharolobus solfataricus
78
-
 5 min, 50% residual activity, mutant enzyme C259S/C261S/C262S/C200S/C205S/C138S Saccharolobus solfataricus
91
-
 5 min, 50% residual activity, mutant enzyme C259S/C261S/C262S Saccharolobus solfataricus
102
-
 5 min, 50% residual activity, mutant enzyme C259S/C261S Saccharolobus solfataricus
106
-
 5 min, 50% residual activity, mutant enzyme C262S Saccharolobus solfataricus
112
-
 5 min, 50% residual activity, wild-type enzyme Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Saccharolobus solfataricus