How Enzymes Work

@article{Ringe2008HowEW,
  title={How Enzymes Work},
  author={Dagmar Ringe and Gregory A. Petsko},
  journal={Science},
  year={2008},
  volume={320},
  pages={1428 - 1429}
}
Fifty years of research have led to a detailed understanding of the mechanisms of enzymatic catalysis. 
Quo vadis, enzymology?
  • C. Khosla
  • Biology, Medicine
  • Nature chemical biology
  • 2015
Enzymology has been a vital link between chemistry and biology in the second half of the twentieth century. A range of emerging scientific challenges is presenting the field with excitingExpand
Nature-inspired design and synthesis of heterogeneous and macromolecular catalysts
Advances in understanding enzyme catalysis have made possible development of synthetic schemes and strategies to incorporate the essential functions of enzymes into artificial structures. Two ofExpand
Rational Design of Bioinspired Catalysts for Selective Oxidations
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TLDR
Here, the efforts made in the last years to model catalysis in post-transcriptional and post- translational processes are reviewed and the advantages and problems of the different computational strategies and their applicability in different cases are stressed. Expand
Molecular protection of fatty acid methyl esters within a supramolecular capsule.
TLDR
A supramolecular nano-capsule is used for selective protection of cis- and trans-C18 mono-unsaturated fatty-acid esters and protection was found to be dependent on the packing motif of the guest. Expand
Transforming a Stable Amide into a Highly Reactive One: Capturing the Essence of Enzymatic Catalysis.
TLDR
The kinetic results are consistent with spatiotemporal concepts where embedding the amide group between two carboxylic moieties in proper geometries, at distances less than the diameter of water, leads to enzyme-like rate enhancements. Expand
Reversible photoresponsive activity of a carbonic anhydrase mimic.
TLDR
An active site mimic that offers reversible control of the catalytic activity using light and was demonstrated that the CA-activity was further enhanced by stabilizing the transition state with the cis-form of the enzyme mimic which can catalyze the hydration of gaseous CO2. Expand
A “Diels‐Alderase” at Last
  • C. Townsend
  • Chemistry, Medicine
  • Chembiochem : a European journal of chemical biology
  • 2011
TLDR
A cycloaddition catalyzed by a monofunctional "Diels-Alderase" has been characterized and a 500-fold rate enhancement shown by this enzyme stack up. Expand
Enzymatic functionalization of carbon-hydrogen bonds.
TLDR
The most prevalent mechanistic strategies used by enzymes to functionalize non-acidic C-H bonds are discussed, the application and evolution of these enzymes for chemical synthesis, and a number of potential biosynthetic capabilities uniquely enabled by these powerful catalysts are discussed. Expand
From Active Sites to Machines: A Challenge for Enzyme Chemists.
  • C. Khosla
  • Chemistry, Medicine
  • Israel journal of chemistry
  • 2019
As researchers who study enzyme chemistry embrace increasingly complex systems, especially biological machines, our attention is also shifting from steps involving covalent bond formation or cleavageExpand
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The promise of advancing and integrating cutting edge conceptual, experimental, and computational tools brings mechanistic enzymology to a new era, one poised for novel fundamental insights into biological catalysis. Expand
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The atomic-resolution structure of a high-energy reaction intermediate stabilized in the active site of an enzyme is reported, revealing a stabilized pentacovalent phosphorane formed in the phosphoryl transfer from the C(1)O of glucose 1,6-(bis)phosphate to the nucleophilic Asp8 carboxylate. Expand
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It is proposed that geometrical complementarity between theOxyanion hole hydrogen-bond donors and the transition state oxyanion provides a significant catalytic contribution, and it is suggested that KSI, like other enzymes, achieves its catalytic prowess through a combination of modest contributions from several mechanisms rather than from a single dominant contribution. Expand
The Low Barrier Hydrogen Bond in Enzymatic Catalysis*
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This minireview will explain the original proposal, summarize the experimental data from the past few years, and argue that LBHBs do play important roles in enzymatic reactions. Expand
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The mutant enzyme can no longer prevent the loss of the enediol phosphate from the active site and its rapid decomposition to methylglyoxal and inorganic phosphate. Expand
Chemical basis for enzyme catalysis.
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A description and analysis of the enzyme -substrate complex characteristics are a focus of this review and it is noted that the narrow range of log kcat values does not correlate. Expand
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