The Enzyme Database

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EC 4.2.99.18     
Accepted name: DNA-(apurinic or apyrimidinic site) lyase
Reaction: The C-O-P bond 3′ to the apurinic or apyrimidinic site in DNA is broken by a β-elimination reaction, leaving a 3′-terminal unsaturated sugar and a product with a terminal 5′-phosphate
Other name(s): AP lyase; AP endonuclease class I; endodeoxyribonuclease (apurinic or apyrimidinic); deoxyribonuclease (apurinic or apyrimidinic); E. coli endonuclease III; phage-T4 UV endonuclease; Micrococcus luteus UV endonuclease; AP site-DNA 5′-phosphomonoester-lyase; X-ray endonuclease III
Systematic name: DNA-(apurinic or apyrimidinic site) 5′-phosphomonoester-lyase
Comments: 'Nicking' of the phosphodiester bond is due to a lyase-type reaction, not hydrolysis. This group of enzymes was previously listed as endonucleases, under EC 3.1.25.2.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 61811-29-8
References:
1.  Bailly, V., Sente, B. and Verly, W.G. Bacteriophage-T4 and Micrococcus luteus UV endonucleases are not endonucleases but β-elimination and sometimes -elimination catalysts. Biochem. J. 259 (1989) 751–759. [PMID: 2471512]
2.  Bailly, V. and Verly, W.G. Escherichia coli endonuclease III is not an endonuclease but a β-elimination catalyst. Biochem. J. 242 (1987) 565–572. [PMID: 2439070]
3.  Bailly, V. and Verly, W.G. AP endonucleases and AP lyases. Nucleic Acids Res. 17 (1989) 3617–3618. [PMID: 2471157]
4.  Manoharan, M., Mazumder, A., Ransom, S.C., Gerlt, J.A. and Bolton, P.H. Mechanism of UV endonuclease-V cleavage of abasic sites in DNA determined by C-13 labeling. J. Am. Chem. Soc. 110 (1988) 2690–2691.
[EC 4.2.99.18 created 1978 as EC 3.1.25.2, transferred 1992 to EC 4.2.99.18]
 
 


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