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

BRENDA support

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

Engineering

Engineering on EC 3.2.2.1 - purine nucleosidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C253A
kcat/KM values for the hydrolysis of inosine, adenosine and guanosine are reduced by a factor of about 120fold compared to the wild-tpe enzyme
C42A
the kcat/KM values for the hydrolysis of inosine, adenosine, and guanosine are reduced by a factor of about 14-, 22-, and 10fold, respectively, compared to the wild-type enzyme
D250A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D252A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D25A
site-directed mutagenesis, inactive mutant
E247A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H245A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H99A
site-directed mutagenesis, inactive mutant
Y241A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y244A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y249A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y255A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D250A
Physcomitrium patens Gransden 2004
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
D252A
Physcomitrium patens Gransden 2004
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
H99A
Physcomitrium patens Gransden 2004
-
site-directed mutagenesis, inactive mutant
-
Y249A
Physcomitrium patens Gransden 2004
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
H79A
kcat/Km for inosine is 13fold lower than wild-type value
L221Y/N228V
site-directed mutagenesis, altered substrate specificity and cleavage pattern, as well as catalytic efficiency compared to the wild-type enzyme
H79A
-
kcat/Km for inosine is 13fold lower than wild-type value
-
C248P
mutant shows decreased kcat value compared to the wild type enzyme using guanosine as substrate
D253P
mutant shows increased kcat value compared to the wild type enzyme using guanosine as substrate
E249P
mutant shows decreased kcat value compared to the wild type enzyme using guanosine as substrate
H247P
mutant shows increased kcat value compared to the wild type enzyme using guanosine as substrate
L250P
mutant shows decreased kcat value compared to the wild type enzyme using guanosine as substrate
L251P
mutant shows increased kcat value compared to the wild type enzyme using guanosine as substrate
R252P
mutant shows increased kcat value compared to the wild type enzyme using guanosine as substrate
D8A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
additional information