3.1.27.8: Ribonuclease V
This is an abbreviated version!
For detailed information about Ribonuclease V, go to the full flat file.
Word Map on EC 3.1.27.8
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3.1.27.8
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pyrimidine
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deaminate
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nick
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dimer-specific
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deoxyinosine
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phosphodiester
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cyclobutane
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repair-deficient
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inosine-containing
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abasic
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dimer-containing
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incises
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deoxyinosine-containing
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n-glycosylase
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cis-syn
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dna-interactive
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uracil-containing
- 3.1.27.8
- pyrimidine
-
deaminate
- nick
-
dimer-specific
- deoxyinosine
-
phosphodiester
-
cyclobutane
-
repair-deficient
-
inosine-containing
-
abasic
-
dimer-containing
-
incises
-
deoxyinosine-containing
-
n-glycosylase
-
cis-syn
-
dna-interactive
-
uracil-containing
Reaction
hydrolysis of poly(A), forming oligoribonucleotides and ultimately 3'-AMP =
Synonyms
endonuclease V, EndoV, FLJ35220, FLJ35220 protein, hEndoV
ECTree
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Engineering
Engineering on EC 3.1.27.8 - Ribonuclease V
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C225S
site-directed mutagenesis, the mutant shows significantly reduced enzyme activity compared to the wild-type full-length enzyme
C226S
site-directed mutagenesis, the mutant shows significantly reduced enzyme activity compared to the wild-type full-length enzyme
C227S
site-directed mutagenesis, the mutant shows significantly reduced enzyme activity compared to the wild-type full-length enzyme
C228S
site-directed mutagenesis, the mutant shows significantly reduced enzyme activity compared to the wild-type full-length enzyme
D52A
site-directed mutagenesis of an active site residue, inactive mutant
E100A
site-directed mutagenesis of an active site residue, the mutant shows highly reduced activity compared to the wild-type enzyme
Y91A
site-directed mutagenesis of an active site residue, the mutant shows highly reduced activity compared to the wild-type enzyme
additional information
construction of truncated enzyme version representing residues Thr13-Ser250, i.e. hEndoV-SF. The mutant shows reduced enzyme activity compared to the wild-type full-length enzyme
additional information
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construction of truncated enzyme version representing residues Thr13-Ser250, i.e. hEndoV-SF. The mutant shows reduced enzyme activity compared to the wild-type full-length enzyme