The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
The metabolism of neuropeptides. The hydrolysis of peptides, including enkephalins, tachykinins and their analogues, by endopeptidase-24.11
Open accessAbstract
Endopeptidase-24.11 (EC 3.4.24.11), purified to homogeneity from pig kidney, was shown to hydrolyse a wide range of neuropeptides, including enkephalins, tachykinins, bradykinin, neurotensin, luliberin and cholecystokinin. The sites of hydrolysis of peptides were identified, indicating that the primary specificity is consistent with hydrolysis occurring at bonds involving the amino group of hydrophobic amino acid residues. Of the substrates tested, the amidated peptide substance P is hydrolysed the most efficiently (Km = 31.9 microM; kcat. = 5062 min-1). A free alpha-carboxy group at the C-terminus of a peptide substrate is therefore not essential for efficient hydrolysis by the endopeptidase. A large variation in kcat./Km values was observed among the peptide substrates studied, a finding that reflects a significant influence of amino acid residues, remote from the scissile bond, on the efficiency of hydrolysis. These subsite interactions between peptide substrate and enzyme thus confer some degree of functional specificity on the endopeptidase. The inhibition of endopeptidase-24.11 by several compounds was compared with that of pig kidney peptidyldipeptidase A (EC 3.4.15.1). Of the inhibitors examined, only N-[1(R,S)-carboxy-2-phenylethyl]-Phe-p-aminobenzoate inhibited endopeptidase-24.11 but not peptidyldipeptidase. Captopril (D-3-mercapto-2-methylpropanoyl-L-proline), Teprotide (pGlu-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro) and MK422 [N-[(S)-1-carboxy-3-phenylpropyl]-L-Ala-L-Pro] were highly selective as inhibitors of peptidyldipeptidase. Although not wholly specific, phosphoramidon was a more potent inhibitor of endopeptidase-24.11 than were any of the synthetic compounds tested.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Proteinases in mammalian cells and tissues
Kerr, M. (1978) · Biochemical Education · doi:10.1016/0307-4412(78)90169-3 · Cited by 919
The enkephalinase inhibitor thiorphan shows antinociceptive activity in mice
Roques, B. P., Fournié-Zaluski, M. C., Soroca, E., Lecomte, J. M., Malfroy, B., Llorens, C., & Schwartz, J.-C. (1980) · Nature · doi:10.1038/288286a0 · Cited by 705
A new class of angiotensin-converting enzyme inhibitors
Patchett, A. A., Harris, E., Tristram, E. W., Wyvratt, M. J., Wu, M. T., Taub, D., Peterson, E. R., Ikeler, T. J., ten Broeke, J., Payne, L. G., et al. (1980) · Nature · doi:10.1038/288280a0 · Cited by 699
High-affinity enkephalin-degrading peptidase in brain is increased after morphine
MALFROY, B., SWERTS, J. P., GUYON, A., ROQUES, B. P., & SCHWARTZ, J. C. (1978) · Nature · doi:10.1038/276523a0 · Cited by 642
The purification and specificity of a neutral endopeptidase from rabbit kidney brush border
Kerr, M. A., & Kenny, A. J. (1974) · Biochemical Journal · doi:10.1042/bj1370477 · Cited by 460
Self-citationSchwartz, J.-C., Malfroy, B., & De La Baume, S. (1981) · Life Sciences · doi:10.1016/0024-3205(81)90182-x · Cited by 381
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
Self-citationProteolysis in Neuropeptide Processing and Other Neural Functions
Loh, Y. P., Brownstein, M. J., & Gainer, H. (1984) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.07.030184.001201 · Cited by 263
Fulcher, I. S., Matsas, R., Turner, A. J., & Kenny, A. J. (1982) · Biochemical Journal · doi:10.1042/bj2030519 · Cited by 172
Self-citationPurification and specificity of a membrane-bound metalloendopeptidase from bovine pituitaries
Orlowski, M., & Wilk, S. (1981) · Biochemistry · doi:10.1021/bi00520a021 · Cited by 163
Cited by
Papandreou, C. N., Usmani, B., Geng, Y., Bogenrieder, T., Freeman, R., Wilk, S., Finstad, C. L., Reuter, V. E., Powell, C. T., Scheinberg, D., et al. (1998) · Nature Medicine · doi:10.1038/nm0198-050 · Cited by 277
Welches, W. R., Bridget Brosnihan, K., & Ferrario, C. M. (1993) · Life Sciences · doi:10.1016/0024-3205(93)90108-f · Cited by 254
The kallikrein-kininogen-kinin system: lessons from the quantification of endogenous kinins
Blais, C., Marceau, F., Rouleau, J.-L., & Adam, A. (2000) · Peptides · doi:10.1016/s0196-9781(00)00348-x · Cited by 135
Gao, B., Vavricka, S. R., Meier, P. J., & Stieger, B. (2015) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-014-1596-x · Cited by 100
Tachykinins and tachykinin receptors in human uterus
Patak, E., Luz Candenas, M., Pennefather, J. N., Ziccone, S., Lilley, A., Martín, J. D., Flores, C., Mantecón, A. G., Story, M. E., & Pinto, F. M. (2003) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705279 · Cited by 82
Metadata
- Authors
- Matsas, R., Kenny, A. J., & Turner, A. J.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1984-10-15
- Volume
- 223
- Issue
- 2
- Pages
- 433-440
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1896060457
- Cited by
- 370
- References
- 18
- FWCI
- 9.67
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: The metabolism of neuropeptides. The hydrolysis of peptides, including enkephalins, tachykinins and their analogues, by endopeptidase-24.11. https://app.cochat.ai/papers/10.1042/bj2230433
- The paper
- Matsas, R., Kenny, A. J., & Turner, A. J. (1984). The metabolism of neuropeptides. The hydrolysis of peptides, including enkephalins, tachykinins and their analogues, by endopeptidase-24.11. Biochemical Journal. https://doi.org/10.1042/bj2230433
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
