Enzyme-catalyzed phosphoryl transfer reactions.

  title={Enzyme-catalyzed phosphoryl transfer reactions.},
  author={Jeremy R. Knowles},
  journal={Annual review of biochemistry},
  • J. Knowles
  • Published 1980
  • Chemistry, Biology
  • Annual review of biochemistry
PERSPECTIVES AND SUMMARY ... 877 Classes of enzyme involving reactions at phosphorus 878 COVALENT REACTION INTERMEDIATES, CRYPTIC AND OTHERWISE 879 Reactions of Phosphoric Monoesters ..... 879 Phosphatoses ..... ..... 879 Phosphokinases • •..•.....• • 881 Phosphomutases 886 Reactions of Phosphoric Diesters 890 REACTION ENERGETICS 892 "Off" Rates 893 Internal Thermodynamics ... .. ... ..... ...... ...... ... 896 THE NATURE OF THE ELEMENTARY STEP ....... ...... 898 Associative versus Diss… 
Snapshot of a phosphorylated substrate intermediate by kinetic crystallography.
A key feature in the structure of the complex of the enzyme with the reaction intermediate is two magnesium ions, bridging the phosphates at the cleavage site, which compensate the negative charges at both phosphate groups after phosphoryl transfer and contribute to the stabilization of the Reaction intermediate.
Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: role of divalent metals in the dimerization and phosphorylation of enzyme I.
The stability of the dimer was also strongly dependent on salts such as LiCl, NaCl, KCl, and a series of tetraalkylammonium chlorides, which suggest that hydrophobic interactions possibly play a significant role in enzyme I dimerization.
Enzymatic and chemical reactivities of sym-monothiopyrophosphate
Observations of the synthesis of sym-monothiopyrophosphate are consistent with the transition states for these enzymes being dissociative in nature, although they do not prove that they are Dissociative.
QM/MM studies of phosphoryl transfer reactions in Alkaline Phosphatase superfamily
Members in the Alkaline Phosphatase (AP) superfamily demonstrate amazing catalytic specificity and promiscuity for a wide range of substrates. In particular, AP and Nucleotide
The substrate reactivity of mu-monothiopyrophosphate with pyrophosphate-dependent phosphofructokinase: evidence for a dissociative transition state in enzymatic phosphoryl group transfer.
A modified synthesis and purification of MTP are described, in which (trimethylsilyl)trifluoromethanesulfonate and tetra-N-butylammonium iodide are used in place of iodotrimethylsilane to dealkylate tetramethyl-MTP, and results are interpreted to indicate a dissociative transition state for PPi-dependent PFK.
Structure-activity relationships in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta.
The mechanism and substrate specificity of the phosphotriesterase from Pseudomonas diminuta have been examined and the inhibition patterns by the products are consistent with a random kinetic mechanism.
Stereochemical course of the reactions catalyzed by the bacterial phosphoenolpyruvate:mannitol phosphotransferase system.
The results imply that EIIMtl is sequentially phosphorylated at two different sites during phospho transfer from phospho-HPr to mannitol.