Literature summary for 3.1.21.7 extracted from

Rosnes, I.; Rowe, A.D.; Vik, E.S.; Forstrom, R.J.; Alseth, I.; Bjoras, M.; Dalhus, B.
Structural basis of DNA loop recognition by endonuclease V (2013), Structure, 21, 257-265.

Search for more literature for 3.1.21.7

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with DNA containing one nucleotide A:TT loop, vapor diffusion method, using 15% (w/v) polyethylene glycol 400 and 100 mM MES, pH 6.3	Thermotoga maritima

Protein Variants

Protein Variants	Comment	Organism
D43A	active site mutant	Thermotoga maritima

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
DNA + H2O	Thermotoga maritima	the enzyme binds A:TT loops with higher affinity than undamaged DNA	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Thermotoga maritima	Q9X2H9	-	-

Purification (Commentary)

Purification (Comment)	Organism
HiTrap SP column chromatography, and Superdex 75 gel filtration	Thermotoga maritima

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
DNA + H2O	the enzyme binds A:TT loops with higher affinity than undamaged DNA	Thermotoga maritima	?	-	?

Synonyms

Synonyms	Comment	Organism
endonuclease V	-	Thermotoga maritima
EndoV	-	Thermotoga maritima

General Information

General Information	Comment	Organism
physiological function	the DNA repair enzyme recognizes and cleaves DNA at deaminated adenine lesions (hypoxanthine) In addition, the enzyme cleaves DNA containing various helical distortions such as loops, hairpins, and flaps	Thermotoga maritima

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Release 2023.1 (January 2023)