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Literature summary extracted from

  • Feng, H.; Dong, L.; Klutz, A.M.; Aghaebrahim, N.; Cao, W.
    Defining amino acid residues involved in DNA-protein interactions and revelation of 3'-exonuclease activity in endonuclease V (2005), Biochemistry, 44, 11486-11495.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.1.21.7 A123I levels of oxanosine and uridine cleavage are reduced by more than 90% Thermotoga maritima
3.1.21.7 A138I mutation reduces level of T/I cleavage by 10% Thermotoga maritima
3.1.21.7 A86M fully active in inosine and xanthosine substrates, significant loss in the level of oxanosine and uridine cleavage Thermotoga maritima
3.1.21.7 F46A mutation reduces the levels of oxanosine and uridine cleavage to less than 40% Thermotoga maritima
3.1.21.7 F87A mutant essentially maintains wild-type level activity towards inosine, xanthosine, oxanosine and uridine substrates Thermotoga maritima
3.1.21.7 G111V levels of oxanosine and uridine cleavage are reduced by more than 90%, level of cleavage of the T/I substrate is reduced by 40% Thermotoga maritima
3.1.21.7 G113V levels of oxanosine and uridine cleavage are reduced by more than 90%, level of cleavage of the T/I substrate is reduced by 50% Thermotoga maritima
3.1.21.7 G121V levels of oxanosine and uridine cleavage are reduced by more than 90%, level of cleavage of the T/I substrate is reduced by 10% Thermotoga maritima
3.1.21.7 G127V levels of oxanosine and uridine cleavage are reduced by more than 90%, level of cleavage of the T/I substrate is reduced by 70% Thermotoga maritima
3.1.21.7 G184V mutation reduces the level of inosine and xanthosine cleavage Thermotoga maritima
3.1.21.7 G41V mutation reduces the levels of oxanosine and uridine cleavage to less than 40% Thermotoga maritima
3.1.21.7 G83V fully active in inosine and xanthosine substrates, significant loss in the level of oxanosine and uridine cleavage Thermotoga maritima
3.1.21.7 H125A significant activities on all substrates Thermotoga maritima
3.1.21.7 I81A mutant essentially maintains wild-type level activity towards inosine, xanthosine and uridine substrates, 40% less active towards oxanosine substrates Thermotoga maritima
3.1.21.7 K139A mutation reduces level of T/I cleavage by 10% Thermotoga maritima
3.1.21.7 K139Q mutation reduces level of T/I cleavage by 10% Thermotoga maritima
3.1.21.7 K139R mutation reduces level of T/I cleavage by 10% Thermotoga maritima
3.1.21.7 L85V fully active in inosine and xanthosine substrates, significant loss in the level of oxanosine and uridine cleavage Thermotoga maritima
3.1.21.7 P207A mutant maintains significant activity towards all substrates Thermotoga maritima
3.1.21.7 P209A mutant maintains significant activity towards all substrates Thermotoga maritima
3.1.21.7 P79A mutant essentially maintains wild-type level activity towards inosine, xanthosine, oxanosine and uridine substrates Thermotoga maritima
3.1.21.7 P82A mutant essentially maintains wild-type level activity towards inosine, xanthosine, oxanosine and uridine substrates, 70% less active towards oxanosine substrates Thermotoga maritima
3.1.21.7 R211A mutant maintains significant activity towards all substrates Thermotoga maritima
3.1.21.7 R211K mutant maintains significant activity towards all substrates Thermotoga maritima
3.1.21.7 R88E fully active in inosine and xanthosine substrates, significant loss in the level of oxanosine and uridine cleavage Thermotoga maritima
3.1.21.7 R99Q fully active in inosine and xanthosine substrates, significant loss in the level of oxanosine and uridine cleavage Thermotoga maritima
3.1.21.7 V137A mutation reduces level of T/I cleavage by 10% Thermotoga maritima
3.1.21.7 Y80A mutant is fully active towards inosine and xanthosine substrates but is minimally active on oxanosine and uridine substrates Thermotoga maritima
3.1.21.7 Y80F mutant is fully active towards inosine and xanthosine substrates but is minimally active on oxanosine and uridine substrates, partially active on G/U substrate Thermotoga maritima
3.1.21.7 Y80H mutant is fully active towards inosine and xanthosine substrates but is minimally active on oxanosine and uridine substrates Thermotoga maritima

Organism

EC Number Organism UniProt Comment Textmining
3.1.21.7 Thermotoga maritima
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.21.7 additional information 3'-exonuclease activity in endonuclease V might be preferentially triggered by the specific cleavage event at the inosine site Thermotoga maritima ?
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