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Literature summary for 3.1.21.7 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
Search for more literature for 3.1.21.7

Protein Variants

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

Organism

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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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