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- W2077006909 abstract "The active site regions of thermolysin (TLN) and carboxypeptidase A (CPA) are directly compared by superimposition of the published crystal structures of eight TLN/inhibitor complexes and four CPA-inhibitor complexes. There is a remarkable similarity in the S′1 region of these two zinc metalloenzymes, and it is suggested that this may be a common feature among other enzymes of this class, including the enkephalin-degrading neutral endopeptidase or “enkephalinase” (NEP-24.11). Assuming this common feature, the possible geometry of the S′2 region of enkephalinase was determined by performing classical potential energy calculations on potent NEP-24.11 inhibitors. The active conformation of these inhibitors was thus identified as similar to that found in the X-ray crystal structure of TLN/inhibitor complexes. It is proposed that the active site region of TLN should serve as a reasonable model for that of NEP-24.11. Extension of the model to the case of angiotensin-converting enzyme (ACE) showed that this enzyme might have a similar S′1 region to the other three enzymes, and allowed further definition of the ACE model previously developed in our laboratory." @default.
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- W2077006909 date "1988-01-01" @default.
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- W2077006909 title "Molecular Modelling of the Active Site of Enkephalin-Degrading Neutral Endopeptidase-24.11 (Enkephalinase) An Active Site Model for Neutral Endopeptidase-24.11" @default.
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- W2077006909 doi "https://doi.org/10.1002/qsar.19880070102" @default.
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