C-O Lyases

Base excision repair (BER) is the predominant system correcting simple DNA base lesions formed by oxidation or other DNA damaging agents. Repair of apurinic/apyrimidinic (AP) sites arising in the genome spontaneously or as intermediates of BER is critical owing to their toxic and mutagenic effects. The mammalian apurinic/apyrimidinic endonuclease APE1 (EC 4.2.99.18) is a Mg2+-dependent multifunctional protein operating in protection of cells from oxidative stress via its DNA repair, redox, and transcription regulatory activities. The human AP endonuclease APE1, also called Ref-1 is the major and crucial enzyme for the recognition and processing of AP sites in the base excision repair (BER) of DNA[1]. APE1 operates by incising the DNA phosphodiester backbone 5′ to AP sites, generating a nick with 3′-hydroxyl and 5′-deoxyribose phosphate (dRP) termini. Repair of the resulting nick is completed by DNA polymerase and DNA ligase. In addition to its endonuclease activity, APE1 is known to have 3′-phosphodiesterase and 3′-phosphatase activity and 3′ to 5′ exonuclease activity as well as a role in regulating the redox state of several transcription factors[2].


[1] S.Madlenera et al. Essential role for mammalian apurinic/apyrimidinic (AP) endonuclease Ape1/Ref-1 in telomere maintenance. PNAS 2013, publ. online before print.
[2] K.M. Schermerhorn, S. Delaney. Transient-State Kinetics of Apurinic/Apyrimidinic (AP) Endonuclease 1 Acting on an Authentic AP Site and Commonly Used Substrate Analogs: The Effect of Diverse Metal Ions and Base Mismatches. Biochem. 2013, 52, 7669-7677.

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Axon ID Name Description From price
2137 APE1 Inhibitor III Inhibitor of apurinic/apyrimidinic endonuclease 1 (APE1) €105.00
2136 AR03 Inhibitor of apurinic/apyrimidinic endonuclease 1 (APE1) €105.00

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