| 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, Gene, 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 β δ-elimination catalysts. Biochem. J. 259 (1989) 751–759. [DOI] [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. [DOI] [PMID: 2439070] |
| 3. |
Bailly, V. and Verly, W.G. AP endonucleases and AP lyases. Nucleic Acids Res. 17 (1989) 3617–3618. [DOI] [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. [DOI] |
|
| [EC 4.2.99.18 created 1978 as EC 3.1.25.2, transferred 1992 to EC 4.2.99.18] |
| |
|
| |
|
Printable version