Reactome | APEX1 mediates endonucleolytic cleavage at the 5' side of the AP site

APEX1 mediates endonucleolytic cleavage at the 5' side of the AP site

Stable Identifier

R-HSA-110359

Type

Reaction [transition]

Species

Homo sapiens

Compartment

nucleoplasm

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

APEX1 mediates endonucleolytic cleavage at the 5' side of the AP site

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

APEX1 (APE1, HAP1), a DNA apurinic/apyrimidinic (AP) site DNA lyase, cleaves the DNA strand sugar-phosphate backbone 5' to the AP site generated by DNA glycosylases or that forms by spontaneous loss of a base, producing a DNA strand with a 3'-terminal unsaturated sugar and a DNA strand with a terminal abasic 5'-deoxyribosephosphate (5'-dRP) as cleavage products (Wilson et al. 1995, Bennett et al. 1997, Masuda et al. 1998, Parikh et al. 1998).

Literature References

PubMed ID	Title	Journal	Year
9724657	Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA Tainer, JA, Bharati, S, Krokan, HE, Mol, CD, Slupphaug, G, Parikh, SS	EMBO J	1998
9207062	Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway. Wilson, DM, Wong, D, Bennett, RA, Demple, B	Proc Natl Acad Sci U S A	1997
7608159	Incision activity of human apurinic endonuclease (Ape) at abasic site analogs in DNA Wilson, DM, Grollman, AP, Demple, B, Takeshita, M	J. Biol. Chem.	1995
9804798	Dynamics of the interaction of human apurinic endonuclease (Ape1) with its substrate and product. Bennett, RA, Demple, B, Masuda, Y	J Biol Chem	1998