Purification and characterization of Drosophila melanogaster photolyase.
Animal-type photolyases have very limited sequence homology to microbial-type photolyases. We wanted to find out whether the two types of enzymes have different or similar biochemical and photochemical properties. In particular, the chromophore/cofactor composition of animal photolyases is of special interest since the presence and nature of a second chromophore in these enzymes are not known in contrast to the microbial photolyases which contain FAD cofactor, and folate or deazaflavin as second chromophores. We overproduced the Drosophila melanogaster photolyase in Escherichia coli using the cloned gene. The enzyme contains FAD and folate and thus belongs in the folate class of enzymes but with an action spectrum peak at 420 nm.
Kim
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ST
Department of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill 27599, USA.
Malhotra
K
K
Ryo
H
H
Sancar
A
A
Todo
T
T
D000042:Absorption; D000818:Animals; D004260:DNA Repair; D004255:Deoxyribodipyrimidine Photo-Lyase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004331:Drosophila melanogaster / Q000201:enzymology*; D004926:Escherichia coli / Q000235:genetics; D005453:Fluorescence; D010777:Photochemistry; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013053:Spectrophotometry / Q000379:methods; D013379:Substrate Specificity
D011994:Recombinant Proteins; D004255:Deoxyribodipyrimidine Photo-Lyase