Bacteriophage-T4 and Micrococcus luteus UV endonucleases are not endonucleases but beta-elimination and sometimes beta delta-elimination catalysts

Bacteriophage-T4 UV endonuclease nicks the C(3')-O-P bond 3' to AP (apurinic or apyrimidinic) sites by a beta-elimination reaction. The breakage of this bond is sometimes followed by the nicking of the C(5')-O-P bond 5' to the AP site, leaving a 3'-phosphate end; delta-elimi...

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Bibliographic Details
Published in:Biochemical journal 1989-05, Vol.259 (3), p.751-759
Main Authors: Bailly, V, Sente, B, Verly, W G
Format: Article
Language:English
Subjects:
Biochemistry
Catalysis
Cell Biology
Deoxyribonuclease IV (Phage T4-Induced)
DNA-(Apurinic or Apyrimidinic Site) Lyase
Endodeoxyribonucleases
Endodeoxyribonucleases - metabolism
Human health sciences
Micrococcus - enzymology
Micrococcus luteus
Molecular Biology
Multienzyme Complexes
Multienzyme Complexes - metabolism
N-Glycosyl Hydrolases
N-Glycosyl Hydrolases - metabolism
Oligonucleotides
Oligonucleotides - metabolism
phage T4
Sciences de la santé humaine
T-Phages - enzymology
UV endonuclease
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Summary:Bacteriophage-T4 UV endonuclease nicks the C(3')-O-P bond 3' to AP (apurinic or apyrimidinic) sites by a beta-elimination reaction. The breakage of this bond is sometimes followed by the nicking of the C(5')-O-P bond 5' to the AP site, leaving a 3'-phosphate end; delta-elimination is proposed as a mechanism to explain this second reaction. The AP site formed when this enzyme acts on a pyrimidine dimer in a polynucleotide chain undergoes the same nicking reactions. Micrococcus luteus UV endonuclease also nicks the C(3')-O-P bond 3' to AP sites by a beta-elimination reaction. No subsequent delta-elimination was observed, but this might be due to the presence of 2-mercaptoethanol in the enzyme preparation.
ISSN:0264-6021
1470-8728
1470-8728
DOI:10.1042/bj2590751