The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Total Chemical Synthesis of a D-Enzyme: The Enantiomers of HIV-1 Protease Show Reciprocal Chiral Substrate Specificity
Abstract
The D and L forms of the enzyme HIV-1 protease have been prepared by total chemical synthesis. The two proteins had identical covalent structures. However, the folded protein-enzyme enantiomers showed reciprocal chiral specificity on peptide substrates. That is, each enzyme enantiomer cut only the corresponding substrate enantiomer. Reciprocal chiral specificity was also evident in the effect of enantiomeric inhibitors. These data imply that the folded forms of the chemically synthesized D- and L-enzyme molecules are mirror images of one another in all elements of the three-dimensional structure. Enantiomeric proteins are expected to display reciprocal chiral specificity in all aspects of their biochemical interactions.
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Cites
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Conserved Folding in Retroviral Proteases: Crystal Structure of Synthetic HIV-1 Protease
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Self-citationSCHNölzer, M., ALEWOOD, P., JONES, A., ALEWOOD, D., & KENT, S. B. H. (1992) · International Journal of Peptide and Protein Research · doi:10.1111/j.1399-3011.1992.tb00291.x · Cited by 1,049
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Cited by
Yashima, E., Ousaka, N., Taura, D., Shimomura, K., Ikai, T., & Maeda, K. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00354 · Cited by 2,004
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Enrichment of the amino acid l -isovaline by aqueous alteration on CI and CM meteorite parent bodies
Glavin, D. P., & Dworkin, J. P. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811618106 · Cited by 307
The Search for Chiral Asymmetry as a Potential Biosignature in our Solar System
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Structures of peptides from α‐amino acids methylated at the α‐carbon,
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Metadata
- Authors
- Milton, R. C. D., Milton, S. C. F., & Kent, S. B. H.
- Venue
- Science
- Published
- 1992-06-05
- Volume
- 256
- Issue
- 5062
- Pages
- 1445-1448
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2027168767
- Cited by
- 425
- References
- 17
- FWCI
- 6.74
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Total Chemical Synthesis of a D-Enzyme: The Enantiomers of HIV-1 Protease Show Reciprocal Chiral Substrate Specificity. https://app.cochat.ai/papers/10.1126/science.1604320
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- Milton, R. C. D., Milton, S. C. F., & Kent, S. B. H. (1992). Total Chemical Synthesis of a D-Enzyme: The Enantiomers of HIV-1 Protease Show Reciprocal Chiral Substrate Specificity. Science. https://doi.org/10.1126/science.1604320
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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