Biology: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 / QuickGO | ||||||||
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In enzymology, a deoxyribodipyrimidine photo-lyase (EC 4.1.99.3) is an enzyme that catalyzes the chemical reaction
- cyclobutadipyrimidine (in DNA) [math]\displaystyle{ \rightleftharpoons }[/math] 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
- "Studies on a DNA photoreactivating enzyme from Streptomyces griseus II. Purification of the enzyme". Biochim. Biophys. Acta 378 (1): 54–63. 1975. doi:10.1016/0005-2787(75)90136-7. PMID 804322.
- "Action mechanism of Escherichia coli DNA photolyase. I. Formation of the enzyme-substrate complex". J. Biol. Chem. 262 (1): 478–85. 1987. PMID 3539939.
- "The minimum size of the substrate for yeast photoreactivating enzyme". Biochim. Biophys. Acta 157 (2): 233–7. 1968. doi:10.1016/0005-2787(68)90077-4. PMID 5649902.
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