Deoxyribodipyrimidine photo-lyase

Deoxyribodipyrimidine photo-lyase
deoxyribodipyrimidine photo-lyase
Identifiers
EC number 4.1.99.3
CAS number 37290-70-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

In enzymology, a deoxyribodipyrimidine photo-lyase (EC 4.1.99.3) is an enzyme that catalyzes the chemical reaction

cyclobutadipyrimidine (in DNA) \rightleftharpoons 2 pyrimidine residues (in DNA)

Hence, this enzyme has one substrate, cyclobutadipyrimidine (in DNA), and one product, pyrimidine residues (in DNA).

This enzyme belongs to the family of lyases, specifically in the "catch-all" class of carbon-carbon lyases. The systematic name of this enzyme class is deoxyribocyclobutadipyrimidine pyrimidine-lyase. Other names in common use include photoreactivating enzyme, DNA photolyase, DNA-photoreactivating enzyme, DNA cyclobutane dipyrimidine photolyase, DNA photolyase, deoxyribonucleic photolyase, deoxyribodipyrimidine photolyase, photolyase, PRE, PhrB photolyase, deoxyribonucleic cyclobutane dipyrimidine photolyase, phr A photolyase, dipyrimidine photolyase (photosensitive), and deoxyribonucleate pyrimidine dimer lyase (photosensitive). It has 2 cofactors: FAD, and 5,10-Methenyltetrahydrofolate.

Structural studies

As of late 2007, 14 structures have been solved for this class of enzymes, with PDB accession codes 1DNP, 1IQR, 1IQU, 1OWL, 1OWM, 1OWN, 1OWO, 1OWP, 1QNF, 1TEZ, 2E0I, 2J07, 2J08, and 2J09.

References

  • Eker AP, Fichtinger-Schepman AM (1975). "Studies on a DNA photoreactivating enzyme from Streptomyces griseus II. Purification of the enzyme". Biochim. Biophys. Acta. 378 (1): 54–63. PMID 804322. 
  • Sancar GB, Smith FW, Reid R, Payne G, Levy M, Sancar A (1987). "Action mechanism of Escherichia coli DNA photolyase. I. Formation of the enzyme-substrate complex". J. Biol. Chem. 262 (1): 478–85. PMID 3539939. 
  • Setlow JK, Bollum FJ (1968). "The minimum size of the substrate for yeast photoreactivating enzyme". Biochim. Biophys. Acta. 157 (2): 233–7. PMID 5649902. 
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