EC 4.1.99.13 - (6-4)DNA photolyase

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IntEnz Enzyme Nomenclature
EC 4.1.99.13

Names

Accepted name:
(6-4)DNA photolyase
Other names:
DNA photolyase
H64PRH
NF-10
phr (6-4)
PL-(6-4)
OtCPF1
(6-4) PHR
At64PHR
Systematic name:
(6-4) photoproduct pyrimidine-lyase

Reactions

Cofactor

Comments:

A flavoprotein (FAD). The overall repair reaction consists of two distinct steps, one of which is light-independent and the other one light-dependent. In the initial light-independent step, a 6-iminium ion is thought to be generated via proton transfer induced by two histidines highly conserved among the (6-4) photolyases. This intermediate spontaneously rearranges to form an oxetane intermediate by intramolecular nucleophilic attack. In the subsequent light-driven reaction, one electron is believed to be transferred from the fully reduced FAD cofactor (FADH-) to the oxetane intermediate thus forming a neutral FADH radical and an anionic oxetane radical, which spontaneously fractures. The excess electron is then back-transferred to the flavin radical restoring the fully reduced flavin cofactor and a pair of pyrimidine bases [2].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00331
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003914
CAS Registry Number: 37290-70-3
UniProtKB/Swiss-Prot:

References

  1. Hitomi, K., DiTacchio, L., Arvai, A. S., Yamamoto, J., Kim, S. T., Todo, T., Tainer, J. A., Iwai, S., Panda, S., Getzoff, E. D.
    Functional motifs in the (6-4) photolyase crystal structure make a comparative framework for DNA repair photolyases and clock cryptochromes.
    Proc. Natl. Acad. Sci. USA 106 : 6962-6967 (2009). [PMID: 19359474]
  2. Schleicher, E., Hitomi, K., Kay, C. W., Getzoff, E. D., Todo, T., Weber, S.
    Electron nuclear double resonance differentiates complementary roles for active site histidines in (6-4) photolyase.
    J. Biol. Chem. 282 : 4738-4747 (2007). [PMID: 17164245]

[EC 4.1.99.13 created 2009]