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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

Inhibitors

Inhibitors on EC 3.1.11.1 - exodeoxyribonuclease I

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-thiophosphorylated oligonucleotide
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camptothecin
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on exposure to camptothecin, depletion of EXO1 in CtIP-deficient cells increases the frequency of DNA-PK-dependent radial chromosome formation
EDTA
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activity 88% reduced in the presence of Mg2+
endonuclease CtIP
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inhibitory effect of CtIP on EXO1 activity using either a radiolabelled DNA oligonucleotide substrate or a linearized plasmid both containing 3'-overhangs
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fullerene-oligonucleotide conjugate
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increasing the amount of cDNA template reduces the inhibitory effect
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NTP
the strong 3'-5' exonuclease activity of polB1 is inhibited by 50% in the presence of 0.002 mM dNTPs, but remains measurable at up to 0.6 mM dNTPs
single-stranded DNA-binding protein
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deleting the N-terminal most Met from the C-terminus of single-stranded DNA-binding protein sequence has a negligible effect on apparent binding to ExoI. The C-terminus of single-stranded DNA-binding proteins abrogate single-stranded DNA-binding protein stimulation of ExoI activity through a competitive inhibition mechanism, the peptides can disrupt ExoI/single-stranded DNA-binding protein/single-stranded DNA ternary complexes. C-terminus of single-stranded DNA-binding protein inhibition is dose-dependent, requiring ca. 0.001 mM peptide to achieve 50% inhibition and ca. 0.01 mM to reduce ExoI activity to C-terminus of single-stranded DNA-binding protein-free levels. Addition of up to 0.1 mM of C-terminus of single-stranded DNA-binding protein does not inhibit ExoI activity to levels below that of ExoI with free single-stranded DNA, and addition of the peptide to single-stranded DNA-binding-protein free reactions has no measurable effect on ExoI nuclease activity
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additional information
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