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3.1.11.1: exodeoxyribonuclease I

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

Word Map on EC 3.1.11.1

Reaction

Exonucleolytic cleavage in the 3'- to 5'- direction to yield nucleoside 5'-phosphates =

Synonyms

3'->5'exonuclease, 3'-to-5' exonuclease, 3'5' exonuclease, 30–50 ssExo, DNA deoxyribophosphodiesterase, DNA polymerase D, DNA polymerase I, dRPase, E. coli exonuclease I, EC 3.1.4.25, Escherichia coli exonuclease I, Exo I, Exo1, EXO1b, ExoA, ExoI, exonuclease 1, exonuclease 1b, exonuclease I, exonuxlease 1, hEXO1, More, OsEXO1, PF2046, PfuExo I, PhoExo I, phosphodiesterase, Pol, Pol BI, POlB1, polD, SbcB15, single-strand DNA 3'-5' exonuclease, single-strand-specific 3'-5' exonuclease, single-stranded DNA-specific 3'-5' exonuclease I, Sso polB1, SSO0552, tthb178, WRN

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.11 Exodeoxyribonucleases producing 5′-phosphomonoesters
                3.1.11.1 exodeoxyribonuclease I

Engineering

Engineering on EC 3.1.11.1 - exodeoxyribonuclease I

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D319A
does not alter the secondary structure significantly. 2-fold binding defect to the C terminus of ssDNA-binding protein relative to wild-type ExoI
E150A
does not alter the secondary structure significantly. 2fold enhanced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
E318A
does not alter the secondary structure significantly. 2fold enhanced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
K227A
does not alter the secondary structure significantly. Displays a 3fold binding defect to the C terminus of ssDNA-binding protein relative to wild-type ExoI
L331A
does not alter the secondary structure significantly. Reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
Q311A
does not alter the secondary structure significantly. Displays modest 2fold binding defect to the C terminus of ssDNA-binding protein relative to wild-type ExoI
R148A
does not alter the secondary structure significantly. Displays dramatically reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
R316A
does not alter the secondary structure significantly. Displays dramatically reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
R327A
does not alter the secondary structure significantly. Reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
R338A
does not alter the secondary structure significantly. Displays a 3fold binding defect to the C terminus of ssDNA-binding protein relative to wild-type ExoI
Y207A
does not alter the secondary structure significantly. Displays dramatically reduced binding to the C terminus of ssDNA-binding protein relative to wild-type ExoI
A153V
the mutation is associated with colorectal cancer and cancer of the small intestine
D173A
E109K
the mutation is associated with colorectal cancer
E589K
the mutation is associated with gastric cancer, lung cancer, hepatocellular carcinoma, melanoma, and glioblastoma
E670G
the mutation is associated with gastric cancer, breast cancer, oral cancer, lung cancer, melanoma, and glioblastoma
F506A
-
substitution on the Mlh1 interacting protein box significantly weakens the interaction with MLH1 and has no impact on the interaction with MSH2 proteins
F506A/F507A
F507A
-
substitution on the Mlh1 interacting protein box significantly weakens the interaction with MLH1 and has no impact on the interaction with MSH2 proteins
N279S
the mutation is associated with breast cancer and pancreatic cancer
P757L
the mutation is associated with colorectal cancer, pancreatic cancer, gastric cancer, breast cancer, oral cancer, lung cancer, and melanoma
Q154A/Y157A
site-directed mutagenesis, the expression of the mutant interferes with S-phase distribution
Q285A/F288A
site-directed mutagenesis, the expression of the mutant interferes with S-phase distribution
R723G/R723S
the mutation is associated with gastric cancer, breast cancer, oral cancer, and lung cancer
S504A
-
substitution on the Mlh1 interacting protein box significantly weakens the interaction with MLH1 and has no impact on the interaction with MSH2 proteins
T439M
the mutation is associated with colorectal cancer
D368A
-
the exonuclease-deficient mutant is drastically impaired for 3'-to-5' exonuclease activity, with no activity detected even at high enzyme-to-DNA substrate ratios
D405A
-
mutant enzyme loses 99.8% of DNA polymerizing activity and 90% of 3'->5' exonucleolytic activity
D405E
-
mutant enzyme loses 95.8% of DNA polymerizing activity and 90% of 3'->5' exonucleolytic activity
DELTAH672-S775
-
mutant enzyme loses 99% of DNA polymerizing activity and 97% of 3'->5' exonucleolytic activity
DELTAL717-S775
-
mutant enzyme loses 97% of DNA polymerizing activity and 97% of 3'->5' exonucleolytic activity
DELTAL746-S775
-
mutant protein has DNA polymerizing activity with 2.3fold higher specific activity than that of the wild-type but retains only 10% of the 3'->5' exonucleolytic activity of the wild-type
D173A
-
site-directed mutagenesis, the exo1-D173A mutant defective in nuclease activity is able to maintain crossing-over at wild-type levels in a number of genetic intervals. Exo1-D173A cells are able to maintain crossing-over despite reducedhDNAformation
F447A
-
abolishes binding to human MLH1
F448A
-
abolishes binding to human MLH1
S445A
-
abolishes binding to human MLH1
D173A
-
site-directed mutagenesis, the exo1-D173A mutant defective in nuclease activity is able to maintain crossing-over at wild-type levels in a number of genetic intervals. Exo1-D173A cells are able to maintain crossing-over despite reducedhDNAformation
-
additional information