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3.2.2.1: purine nucleosidase

This is an abbreviated version!
For detailed information about purine nucleosidase, go to the full flat file.

Word Map on EC 3.2.2.1

Reaction

a purine nucleoside
+
H2O
=
D-ribose
+
a purine base

Synonyms

6-oxopurine nucleosidase, CELE_Y43F8C.13, IAG nucleoside hydrolase, IAG-NH, IAG-nucleoside hydrolase, IAGNH, IG-NH, inosine-adenosine-guanosine nucleoside hydrolase, inosine-adenosine-guanosine-preferring nucleoside hydrolase, inosine-guanosine nucleoside hydrolase, inosine-guanosine-specific nucleoside hydrolase, inosine/adenosine/guanosinepreferring NH, IU-nucleoside hydrolase, IunH, N-ribosyl purine ribohydrolase, N-ribosyl-purine ribohydrolase, NSH3, nucleosidase, nucleosidase g, nucleoside hydrolase, PpNRH1, purine beta-ribosidase, purine hydrolase, purine NRH, Purine nucleosidase, purine nucleoside hydrolase, purine nucleoside N-ribohydrolase, purine ribonucleosidase, purine specific nucleoside hydrolase, purine-preferring nucleoside hydrolase, purine-specific hydrolase, purine-specific inosine-adenosine-guanosine nucleoside hydrolase, purine-specific inosineadenosine-guanosine nucleoside hydrolase, purine-specific NH, purine-specific nucleoside hydrolase, purine-specific ribonucleoside hydrolase, ribonucleoside hydrolase, rih1, rih2, RihC, SsIAG-NH, SslAG-NH, SSO2243, Tb927.3.2960, URH1, URH2, ZmNRH3

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.1 purine nucleosidase

Temperature Stability

Temperature Stability on EC 3.2.2.1 - purine nucleosidase

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100 - 110
-
IAG-NH is characterized by extreme thermodynamic stability with a melting temperature at 107°C, it retains full activity after 1 h incubation at 90°C and shows half-lives of 45 min, 30 min and 15 min at 100°C, 105°C, and 110°C, respectively
108
-
no thermal unfolding transition can be obtained up to 108°C
40
E15229
pH 6.0, 30 min, stable up to
80
-
half-life 5.9 min
93
-
thermally denatured under reducing conditions
additional information