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Comment
. 2002 Feb 22;295(5559):1480-1.
doi: 10.1126/science.1069823.

Enzymology. A moving story

Joseph J Falke  1
Affiliations
Comment

Enzymology. A moving story

Joseph J Falke. Science. .
No abstract available

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Figures

Figure
Figure. Residues in motion
Space-filling atomic structure of the complex between the enzyme cyclophilin A and its substrate cis-Suc-Ala-Phe-Pro-4-NA (20). The substrate is green; residues whose backbone amides detect motional changes due to repetitive substrate binding and dissociation are blue. The catalytic residue arginine 55 is shown in yellow. This residue forms a hydrogen bond to the substrate and detects a motional frequency similar to the catalytic rate, suggesting that it could be involved in motions leading to the formation and decay of the transition state.
See this image and copyright information in PMC

Comment on

  • Enzyme dynamics during catalysis.
    Eisenmesser EZ, Bosco DA, Akke M, Kern D. Eisenmesser EZ, et al. Science. 2002 Feb 22;295(5559):1520-3. doi: 10.1126/science.1066176. Science. 2002. PMID: 11859194

References

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