EC 4.2.99.18 - DNA-(apurinic or apyrimidinic site) lyase

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IntEnz Enzyme Nomenclature
EC 4.2.99.18

Names

Accepted name:
DNA-(apurinic or apyrimidinic site) lyase
Other names:
E. coli endonuclease III
Micrococcus luteus UV endonuclease
AP endonuclease class I
AP lyase
AP site-DNA 5'-phosphomonoester-lyase
X-ray endonuclease III
deoxyribonuclease (apurinic or apyrimidinic)
endodeoxyribonuclease (apurinic or apyrimidinic)
phage-T4 UV endonuclease
Systematic name:
DNA-(apurinic or apyrimidinic site) 5'-phosphomonoester-lyase

Reaction

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 the number EC 3.1.25.2.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00598 , PROSITE:PDOC00599 , PROSITE:PDOC00615
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003906
CAS Registry Number: 61811-29-8
UniProtKB/Swiss-Prot: (628) [show] [UniProt]

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 βδ-elimination catalysts.
    Biochem. J. 259: 751-759 (1989). [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: 565-572 (1987). [PMID: 2439070]
  3. Bailly, V. and Verly, W.G.
    AP endonucleases and AP lyases.
    Nucleic Acids Res. 17: 3617-3618 (1989). [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: 2690-2691 (1988).

[EC 4.2.99.18 created 1978 as EC 3.1.25.2, transferred 1992 to EC 4.2.99.18]