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3.1.21.B1: endonuclease Q

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

Word Map on EC 3.1.21.B1

Reaction

endonucleolytic cleavage of the phosphodiester bond 5' from deoxyinosine, forming a 5'-phosphate terminus and a 3'-hydroxyl terminus. DNAs containing deoxyuridine, 7-deaza-2'-deoxyxanthosine or an apurinic/apyrimidinic site are also cleaved =

Synonyms

BpuEndoQ, EndoQ, PF1551, PfuEndoQ, TK0887

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.21 Endodeoxyribonucleases producing 5'-phosphomonoesters
                3.1.21.B1 endonuclease Q

Engineering

Engineering on EC 3.1.21.B1 - endonuclease Q

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D192A
D193N
endonuclease activity is almost abolished
E76Q
endonuclease activity is almost abolished
H10A
mutant enzyme retaines approximately half of the wild-type endonuclease activity
H139A
endonuclease activity is almost abolished
H84A
endonuclease activity is almost abolished
H8A
mutant enzyme retaines approximately half of the wild-type endonuclease activity
K320A
decreased dsDNA-binding ability
W144A
mutant enzyme with decreased activity
Y244A
mutant shows reduced DNA cleavage activity for the hypoxanthine-containing DNA
Y244F
mutant enzyme cleaves the same DNA more effectively than the wild-type enzyme
Y377A
mutant enzyme cleaves the same DNA more effectively than the wild-type enzyme
Y377F
mutant enzyme cleaves the same DNA more effectively than the wild-type enzyme
E76Q
-
endonuclease activity is almost abolished
-
H139A
-
endonuclease activity is almost abolished
-
H84A
-
endonuclease activity is almost abolished
-
K320A
-
decreased dsDNA-binding ability
-
Y377F
-
mutant enzyme cleaves the same DNA more effectively than the wild-type enzyme
-