Wei Yang1. 1. Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, 9000 Rockville Pike, Building 5, Room B1-03 Bethesda, Maryland 20892, USA. Wei.Yang@nih.gov
Abstract
Nucleotidyl-transfer enzymes, which synthesize, degrade and rearrange DNA and RNA, often depend on metal ions for catalysis. All DNA and RNA polymerases, MutH-like or RNase H-like nucleases and recombinases, and group I introns seem to require two divalent cations to form a complete active site. The two-metal-ion mechanism has been proposed to orient the substrate, facilitate acid-base catalysis and allow catalytic specificity to exceed substrate binding specificity attributable to the stringent metal-ion (Mg2+ in particular) coordination. Not all nucleotidyl-transfer enzymes use two metal ions for catalysis, however. The betabetaalpha-Me and HUH nucleases depend on a single metal ion in the active site for the catalysis. All of these one- and two metal ion-dependent enzymes generate 5'-phosphate and 3'-OH products. Structural and mechanistic comparisons show that these seemingly unrelated nucleotidyl-transferases share a functionally equivalent metal ion.
Nucleotidyl-transfer enzymes, which synthesize, degrade and rearrange Dn class="Chemical">NA and RNA, often depend on metal ions for catalysis. All DNA and RNA polymerases, MutH-like or RNase H-like nucleases and recombinases, and group I introns seem to require two divalent cations to form a complete active site. The two-metal-ion mechanism has been proposed to orient the substrate, facilitate acid-base catalysis and allow catalytic specificity to exceed substrate binding specificity attributable to the stringent metal-ion (Mg2+ in particular) coordination. Not all nucleotidyl-transfer enzymes use two metal ions for catalysis, however. The betabetaalpha-Me and HUH nucleases depend on a single metal ion in the active site for the catalysis. All of these one- and two metal ion-dependent enzymes generate 5'-phosphate and 3'-OH products. Structural and mechanistic comparisons show that these seemingly unrelated nucleotidyl-transferases share a functionally equivalent metal ion.
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