Enzyme-catalyzed phosphoryl transfer reactions.

@article{Knowles1980EnzymecatalyzedPT,
  title={Enzyme-catalyzed phosphoryl transfer reactions.},
  author={Jeremy R. Knowles},
  journal={Annual review of biochemistry},
  year={1980},
  volume={49},
  pages={
          877-919
        }
}
  • 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… 
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Members in the Alkaline Phosphatase (AP) superfamily demonstrate amazing catalytic specificity and promiscuity for a wide range of substrates. In particular, AP and Nucleotide…
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Structure-activity relationships in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta.
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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.
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The results imply that EIIMtl is sequentially phosphorylated at two different sites during phospho transfer from phospho-HPr to mannitol.
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