Escherichia coli photoreactivating enzyme: purification and properties.
We have purified large quantities of Escherichia coli photoreactivating enzyme (EC 4.1.99.3) to apparent homogeneity and have studied its physical and chemical properties. The enzyme has a molecular weight of 36 800 and a S020,W of 3.72 S. Amino acid analysis revealed an apparent absence of tryptophan, a low content of aromatic residues, and the presence of no unusual amino acids. The N terminus is arginine. The purified enzyme contained up to 13% carbohydrate by weight. The carbohydrate was composed of mannose, galactose, glucose, and N-acetylglucosamine. The enzyme is also associated with RNA (approximately 10 nucleotides/enzyme molecule) containing uracil, adenine, guanine, and cytosine with no unusual bases detected.
D000596:Amino Acids / Q000032:analysis; D002241:Carbohydrates / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D004255:Deoxyribodipyrimidine Photo-Lyase / Q000302:isolation & purification* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D006027:Glycosides / Q000032:analysis; D005779:Immunodiffusion; D008190:Lyases / Q000302:isolation & purification*; D008970:Molecular Weight
D000596:Amino Acids; D002241:Carbohydrates; D006027:Glycosides; D008190:Lyases; D004255:Deoxyribodipyrimidine Photo-Lyase