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3.2.2.8: ribosylpyrimidine nucleosidase

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

Word Map on EC 3.2.2.8

Reaction

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

Synonyms

CU-NH, cytidine-uridine nucleoside hydrolase, cytidine-uridine-preferring nucleoside hydrolase, LBRM_18_1610, More, N-ribohydrolase, N-ribosylpyrimidine nucleosidase, N-ribosylpyrimidine ribohydrolase, NH, NSH1, nucleosidase, pyrimidine, nucleoside hydrolase, pyrimidine nucleosidase, pyrimidine nucleoside hydrolase, pyrimidine-specific nucleoside hydrolase, ribonucleoside hydrolase 1, rih1, RihA, RihB, SsCU-NH, SSO0505, URH1, uridine-ribohydrolase 1, YbeK, YeiK

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.8 ribosylpyrimidine nucleosidase

Engineering

Engineering on EC 3.2.2.8 - ribosylpyrimidine nucleosidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H239A
-
dramatic increase in Km for uridine, unchanged kcat
H82N
-
small increase in Km, increase in kcat
Q227A
the mutation causes an increase of kcat for uridine and inosine
Q227F
the mutation causes an increase of kcat for uridine and inosine
Q227Y
the mutation has a strong, enhancing effect on the hydrolysis of inosine, and the catalytic efficiency for the purinic substrate is increased by a factor of 7.6
T223A
the mutation does not improve significantly the catalytic efficiency of YeiK toward inosine
T223F
the mutation does not improve significantly the catalytic efficiency of YeiK toward inosine
T223F/Q227Y
the mutant shows a 2fold increase in catalytic efficiency toward inosine
T223Y
the mutation does not affect the specificity of the enzyme toward inosine or uridine
T223Y/Q227Y
T227A
the mutation does not improve significantly the catalytic efficiency of YeiK toward inosine
T227F
the mutation does not improve significantly the catalytic efficiency of YeiK toward inosine
additional information