Phosphoryl transfer from the high-energy phosphate donor ATP is ubiquitous in biological chemistry, and nitrogen nucleophiles, especially histidine, often serve as in vivo acceptors of the γ-phosphate of ATP. Nevertheless, nonenzymatic reactions of ATP with amines have not previously been characterized. We have therefore examined phosphoryl transfer from ATP to amines to provide a basis for und...

Reversible phosphorylation of proteins is a post-translational modification that regulates diverse biological processes. The molecular mechanism underlying phosphoryl transfer catalyzed by enzymes, in particular the nature of transition state (TS), remains a subject of active debate. Structural evidence supports an associative TS, whereas physical organic studies point to a dissociative charact...

nucleotide was increased, and, assuming that the product was derived from oligonucleotides and deoxyribonucleoside triphosphates, the synthesis amounted to 74% of the deoxyribonucleic acid primer. 4. The nucleotidyltransferase was inhibited and the lag phase extended by 3'-phosphoryl-terminal oligonucleotides from a splenic-deoxyribonuclease digest of deoxyribonucleic acid. 5. The compounds obt...

The phosphoryl group, PO3-, is the dynamic structural unit in the biological chemistry of phosphorus. Its transfer from a donor to an acceptor atom, with oxygen much more prevalent than nitrogen, carbon, or sulfur, is at the core of a great majority of enzyme-catalyzed reactions involving phosphate esters, anhydrides, amidates, and phosphorothioates. The serendipitous discovery that the phospho...

A method is reported for the phosphoryl bond cleavage of O-alkyl phosphinates, phosphinothioates and certain phosphonamidates to furnish the corresponding P(III) borane adducts. The two-step procedure relies upon initial activation of the phosphoryl bond with an alkyl triflate, followed by reduction of the resulting intermediate using lithium borohydride.