Member database | PROSITE patterns |
PROSITE patterns type | conserved site |
Short name | DNA_PHOTOLYASES_2_1 |
Description
Deoxyribodipyrimidine photolyase (EC 4.1.99.3) (DNA photolyase)
[1] is a DNA
repair enzyme. It binds to UV-damaged DNA containing pyrimidine dimers and,
upon absorbing a near-UV photon (300 to 500 nm), breaks the cyclobutane ring
joining the two pyrimidines of the dimer. DNA photolyase is an enzyme that
requires two choromophore-cofactors for its activity: a reduced FADH2 and
either 5,10-methenyltetrahydrofolate (5,10-MTFH) or an oxidized 8-hydroxy-5-
deazaflavin (8-HDF) derivative (F420). The folate or deazaflavin chromophore
appears to function as an antenna, while the FADH2 chromophore is thought to
be responsible for electron transfer. On the basis of sequence similarities
[2] DNA photolyases can be grouped into two classes. The second class contains
enzymes from Myxococcus xanthus, methanogenic archaebacteria, insects, fish
and marsupial mammals. It is not yet known what second cofactor is bound to
class 2 enzymes.
There are a number of conserved sequence regions in all known class 2 DNA
photolyases, especially in the C-terminal part. We selected two of these
regions as signature patterns.
References
1.DNA photorepair: chromophore composition and function in two classes of DNA photolyases. Jorns MS. Biofactors 2, 207-11, (1990). PMID: 2282137
2.A new class of DNA photolyases present in various organisms including aplacental mammals. Yasui A, Eker AP, Yasuhira S, Yajima H, Kobayashi T, Takao M, Oikawa A. EMBO J. 13, 6143-51, (1994). View articlePMID: 7813451