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, Medicine
  • 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… 
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Covalent enzyme-substrate compounds: detection and catalytic competence.
  • D. Purich
  • Chemistry, Medicine
    Methods in enzymology
  • 2002
This chapter summarizes the experimental approaches at the disposal of the enzyme chemist with a focus on covalent enzyme-substrate compounds and the demonstration of their productive participation in catalysis.
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Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: role of divalent metals in the dimerization and phosphorylation of enzyme I.
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Enzymatic and chemical reactivities of sym-monothiopyrophosphate
The synthesis of sym-monothiopyrophosphate (MTP) is described and the relative hydrolysis rate constants are reported for the dianion, trianion, and tetraanion in aqueous solution. The MTP-dianion
8.09 – Phosphoryl and Sulfuryl Transfer
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QM/MM studies of phosphoryl transfer reactions in Alkaline Phosphatase superfamily
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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.