Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.30.2 (endonuclease)
 18,621 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Kinetic studies on the two major isoforms of Serratia marcescens nuclease, Sm2 and Sm1, have revealed them to be functionally equivalent. Both isoforms display marked substrate inhibition by DNA and RNA. They both require magnesium for optimal activity, but retain low catalytic activity in its absence. Both are moderately inhibited by mononucleotides including 5'-ATP, 5'-AMP, 5'-TTP and 3'5'-pTp. The two strongest mononucleotide inhibitors studied, 5'-ATP and 5'-AMP, display inhibition constants, KI, on the order of 10(-5) M. In assessing the strength of mononucleotide inhibition the type of nucleotide base appears to be more important than the number of phosphate moieties.
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PMID:Kinetic studies of the Serratia marcescens extracellular nuclease isoforms. 780 50

The Type I restriction-modification enzymes comprise three protein subunits; HsdS and HsdM that form a methyltransferase (MTase) and HsdR that associates with the MTase and catalyses Adenosine-5'-triphosphate (ATP)-dependent DNA translocation and cleavage. Here, we examine whether the MTase and HsdR components can 'turnover' in vitro, i.e. whether they can catalyse translocation and cleavage events on one DNA molecule, dissociate and then re-bind a second DNA molecule. Translocation termination by both EcoKI and EcoR124I leads to HsdR dissociation from linear DNA but not from circular DNA. Following DNA cleavage, the HsdR subunits appear unable to dissociate even though the DNA is linear, suggesting a tight interaction with the cleaved product. The MTases of EcoKI and EcoAI can dissociate from DNA following either translocation or cleavage and can initiate reactions on new DNA molecules as long as free HsdR molecules are available. In contrast, the MTase of EcoR124I does not turnover and additional cleavage of circular DNA is not observed by inclusion of RecBCD, a helicase-nuclease that degrades the linear DNA product resulting from Type I cleavage. Roles for Type I restriction endonuclease subunit dynamics in restriction alleviation in the cell are discussed.
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PMID:Recycling of protein subunits during DNA translocation and cleavage by Type I restriction-modification enzymes. 2171 44