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Phosphonamidates as transition-state analog inhibitors of thermolysin
Abstract
Six phosphorus-containing peptide analogues of the form Cbz-NHCH2PO2--L-Leu-Y (Y = D-Ala, NH2, Gly, L-Phe, L-Ala, L-Leu) have been prepared and evaluated as inhibitors of thermolysin. The Ki values for these compounds range from 1.7 microM to 9.1 nM and correlate well with the Km/kcat values for the corresponding peptide substrates [Morihara, K., & Tsuzuki, H. (1970) Eur. J. Biochem. 15, 374-380] but not with the Km values alone. The correlation noted between inhibitor Ki and substrate Km/kcat is the most extensive one of this type, providing strong evidence that the phosphonamidates are transition-state analogues and not simply multisubstrate ground-state analogues. Cbz-NH2CH2PO2--L-Leu-L-Leu (Ki = 9.1 nM) is the most potent inhibitor yet reported for thermolysin.
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Metadata
- Authors
- Bartlett, P. A., & Marlowe, C. K.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1983-09-27
- Volume
- 22
- Issue
- 20
- Pages
- 4618-4624
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2076457673
- Cited by
- 265
- References
- 0
- FWCI
- 3.88
- Type
- journal article
- Language
- en
- Open access
- closed
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- Bartlett, P. A., & Marlowe, C. K. (1983). Phosphonamidates as transition-state analog inhibitors of thermolysin. Biochemistry. https://doi.org/10.1021/bi00289a002
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