The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
The lipase inhibitor tetrahydrolipstatin binds covalently to the putative active site serine of pancreatic lipase
Open accessAbstract
Tetrahydrolipstatin (THL) is a selective inhibitor of fat absorption. In animal models, it has anti-obesity and anti-hypercholesterolemic activity and is presently in clinical trials for these indications. THL binds covalently to pancreatic lipase. Complete inhibition of lipolytic activity is obtained concomitant with the incorporation of 1 mol of THL/mol of enzyme. Pancreatic lipase is the best studied lipase, but published results concerning its catalytic mechanism are still controversial. In order to learn more about the inhibitory mechanism of THL, a selective lipase inhibitor interacting at or near the catalytic site, and therefore, to obtain more information on the catalytic mechanism of lipase, we have determined the amino acid residue to which THL is bound. After proteolytic degradation of porcine pancreatic lipase inhibited with radioactively labeled THL, the labeled peptides were isolated and analyzed by quantitative amino acid analysis, N-terminal sequencing, and by mass spectrometry with fast atom bombardment ionization. The data clearly show that THL is bound as an ester to the serine 152 of the lipase.
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Cites
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Buey, R. M., Calvo, E., Barasoain, I., Pineda, O., Edler, M. C., Matesanz, R., Cerezo, G., Vanderwal, C. D., Day, B. W., Sorensen, E. J., et al. (2007) · Nature Chemical Biology · doi:10.1038/nchembio853 · Cited by 156
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Metadata
- Authors
- Hadváry, P., Sidler, W., Meister, W., Vetter, W., & Wolfer, H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1991-02
- Volume
- 266
- Issue
- 4
- Pages
- 2021-2027
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1480098000
- Cited by
- 280
- References
- 16
- FWCI
- 6.80
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: The lipase inhibitor tetrahydrolipstatin binds covalently to the putative active site serine of pancreatic lipase. https://app.cochat.ai/papers/10.1016/s0021-9258(18)52203-1
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- Hadváry, P., Sidler, W., Meister, W., Vetter, W., & Wolfer, H. (1991). The lipase inhibitor tetrahydrolipstatin binds covalently to the putative active site serine of pancreatic lipase. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)52203-1
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