Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 4.2.99.18

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Macromolecule Reactions Polynucleotide-Reactions DNA-Reactions

EC Number: 4.2.99.18

Enzymes and Genes:
endonuclease III; specific for apurinic and/or apyrimidinic sites Inferred from experiment : nth ( Escherichia coli K-12 substr. MG1655 )

Supersedes EC number: 3.1.25.2

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: 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

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: ?

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
Page generated by SRI International Pathway Tools version 18.5 on Sat Nov 22, 2014, biocyc14.