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MetaCyc Reaction: 4.2.99.18

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateMacromolecule ReactionsPolynucleotide-ReactionsDNA-Reactions

EC Number: 4.2.99.18

Enzymes and Genes:

Escherichia coli K-12 substr. MG1655: endonuclease IIIInferred from experiment: nth

Supersedes EC number: 3.1.25.2

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Mass balance status: Balance undetermined; a substrate lacks a chemical formula

Enzyme Commission Primary Name: DNA-(apurinic or apyrimidinic site) lyase

Enzyme Commission Synonyms: 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

Taxonomic Range: Viridiplantae, Fungi, Archaea, Bacteria , Metazoa

Enzyme Commission Summary:
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

'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.

Citations: [Bailly89, Bailly87, Bailly89a]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:4.2.99.18, ENZYME:EC:4.2.99.18, IUBMB-ExplorEnz:EC:4.2.99.18, UniProt:RELATED-TO:P04418, UniProt:RELATED-TO:P0AB83, UniProt:RELATED-TO:P22936, UniProt:RELATED-TO:P23196, UniProt:RELATED-TO:P27695, UniProt:RELATED-TO:P28352, UniProt:RELATED-TO:P43138, UniProt:RELATED-TO:P44319, UniProt:RELATED-TO:P50525, UniProt:RELATED-TO:P95945, UniProt:RELATED-TO:Q9CGM5, UniProt:RELATED-TO:Q9JVT0, UniProt:RELATED-TO:Q9PHS1, UniProt:RELATED-TO:Q9PNL1, UniProt:RELATED-TO:Q58829


References

Bailly87: Bailly V, Verly WG (1987). "Escherichia coli endonuclease III is not an endonuclease but a beta-elimination catalyst." Biochem J 242(2);565-72. PMID: 2439070

Bailly89: Bailly V, Sente B, Verly WG (1989). "Bacteriophage-T4 and Micrococcus luteus UV endonucleases are not endonucleases but beta-elimination and sometimes beta delta-elimination catalysts." Biochem J 259(3);751-9. PMID: 2471512

Bailly89a: Bailly V, Verly WG (1989). "AP endonucleases and AP lyases." Nucleic Acids Res 17(9);3617-8. PMID: 2471157


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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