The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Comparison of the subsite specificity of the mammalian neutral endopeptidase 24.11 (enkephalinase) to the bacterial neutral endopeptidase thermolysin.
Abstract
A comparison has been made of the specificity of the mammalian neutral metalloendopeptidase, endopeptidase 24.11, with that of the bacterial neutral metalloendopeptidase thermolysin. A series of synthetic oligopeptides which have previously been studied as substrates for thermolysin and used in computer modeling were examined as substrates for the mammalian enzyme. It was found that P1, P2, and P'3 subsite interactions in the mammalian enzyme, although similar to those found in thermolysin, are less restrictive spatially and are considerably less dependent on hydrophobic interactions. This difference was maximally expressed with the synthetic substrate dansyl-D-alanylglycylnitrophenylalanylglycine which is a substrate for the mammalian enzyme, but not for the bacterial enzyme. A comparison of substrates in the free acid form with their corresponding amides showed that binding to the mammalian enzyme is dependent in part on an ionic interaction between the substrate carboxylate group and the enzyme. Such an ionic interaction was not observed with the bacterial enzyme.
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“The affinity of neprilysin for its physiological substrates (e.g., enkephalins, tachykinins, atrial natriuretic peptide) and/or different synthetic peptides is in the low millimolar range (68).”
From Clearance of Alzheimer’s amyloid-β1-40 peptide from brain by LDL receptor–related protein-1 at the blood-brain barrier (2000) · cites this paper as [68]
Citations
Cites
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High-affinity enkephalin-degrading peptidase in brain is increased after morphine
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The purification and specificity of a neutral endopeptidase from rabbit kidney brush border
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Hydrolysis of substance P and neurotensin by converting enzyme and neutral endopeptidase
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Matsas, R., Fulcher, I. S., Kenny, A. J., & Turner, A. J. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.10.3111 · Cited by 372
Human kidney "enkephalinase", a neutral metalloendopeptidase that cleaves active peptides
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Self-citationPhosphonamidates as transition-state analog inhibitors of thermolysin
Bartlett, P. A., & Marlowe, C. K. (1983) · Biochemistry · doi:10.1021/bi00289a002 · Cited by 265
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Cited by
Shibata, M., Yamada, S., Kumar, S. R., Calero, M., Bading, J., Frangione, B., Holtzman, D. M., Miller, C. A., Strickland, D. K., Ghiso, J., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10498 · Cited by 1,413
Iwata, N., Tsubuki, S., Takaki, Y., Watanabe, K., Sekiguchi, M., Hosoki, E., Kawashima-Morishima, M., Lee, H.-J., Hama, E., Sekine-Aizawa, Y., et al. (2000) · Nature Medicine · doi:10.1038/72237 · Cited by 867
Clearance of amyloid β-peptide from brain: transport or metabolism?
Zlokovic, B. V., Yamada, S., Holtzman, D., Ghiso, J., & Frangione, B. (2000) · Nature Medicine · doi:10.1038/77397 · Cited by 186
Metadata
- Authors
- Hersh, L. B., & Morihara, K.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1986-05
- Volume
- 261
- Issue
- 14
- Pages
- 6433-6437
- ISSN
- 0021-9258
- Cited by
- 82
- References
- 26
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- creativecommons.org/licenses/by/4.0/ (vor, 12603 d)
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- CoChat. (2026). Citation check: Comparison of the subsite specificity of the mammalian neutral endopeptidase 24.11 (enkephalinase) to the bacterial neutral endopeptidase thermolysin. https://app.cochat.ai/papers/10.1016/s0021-9258(19)84580-5
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- Hersh, L. B., & Morihara, K. (1986). Comparison of the subsite specificity of the mammalian neutral endopeptidase 24.11 (enkephalinase) to the bacterial neutral endopeptidase thermolysin. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)84580-5
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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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