Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.25.1 (deoxyribonuclease)
 1,471 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A deoxyribonuclease has been purified more than 2000-fold from the green algae, Chlamydomonas reinhardii. The enzyme is most active on denatured DNA. Optimum activity is at pH 8.5, in 80 mM Tris-HCl buffer and 2 mM CaCl2. Other divalent cations can replace Ca2+ with varying lower efficiency. EDTA and inorganic phosphate are strongly inhibitory, while ATP and high concentrations of 2-mercaptoethanol are slightly inhibitory. The molecular weight is approximately 35 000, the Stokes radius is 2.7 nm, and the sedimentation coefficient 2.8 S. It is a single polypeptide chain, and the frictional ratio of 1.27 suggests it is only slightly asymetrical. The isoelectric point is 9.5. This enzyme has been termed exonuclease 1.
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PMID:A deoxyribonuclease from Chlamydomonas reinhardii. 1. Purification and properties. 1 43

A deoxyribonuclease purified Chlamydomonas reinhardii has been shown to be specific for single-stranded DNA. The enzyme is most active on thermally denatured DNA, but also degrades single-stranded termini from double-stranded DNA. The enzyme has no effect on single-stranded or double-stranded intact circular phiX174DNA, suggesting that it requires DNA termini for activity. DNA is digested progressively to oligonucleotides and then mononucleotides. The product of the reaction is nucleoside 5'-monophosphates. The enzyme has no effect on RNA, nor does it possess phosphatase or phosphodiesterase activity. No specificity was demonstrated for phosphate or hydroxyl groups at either the 5' or 3' termini of DNA. The enzyme may be able to initiate hydrolysis at either the 3' or the 5' termini, since radioactivity was released more rapidly from 5' and 3' termini than from bulk DNA. The enzyme has been tentatively named Chlamydomonas reinhardii exonuclease 1.
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PMID:A deoxyribonuclease from Chlamydomonas reinhardii. 2. Substrate specificity, mode of action and products. 88 35