The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Calcium-dependent Human Serum Homocysteine Thiolactone Hydrolase
Open accessAbstract
Homocysteine thiolactone is formed in all cell types studied thus far as a result of editing reactions of some aminoacyl-tRNA synthetases. Because inadvertent reactions of thiolactone with proteins are potentially harmful, the ability to detoxify homocysteine thiolactone is essential for biological integrity. This work shows that a single specific enzyme, present in mammalian but not in avian sera, hydrolyzes thiolactone to homocysteine. Human serum thiolactonase, a 45-kDa protein component of high density lipoprotein, requires calcium for activity and stability and is inhibited by isoleucine and penicillamine. Substrate specificity studies suggest that homocysteine thiolactone is a likely natural substrate of this enzyme. However, thiolactonase also hydrolyzes non-natural substrates, such as phenyl acetate, p-nitrophenyl acetate, and the organophospate paraoxon. N-terminal amino acid sequence of pure thiolactonase is identical with that of human paraoxonase. These and other data indicate that paraoxonase, an organophosphate-detoxifying enzyme whose natural substrate and function remained unknown up to now, is in fact homocysteine thiolactonase. By detoxifying homocysteine thiolactone, the thiolactonase/paraoxonase would protect proteins against homocysteinylation, a potential contributing factor to atherosclerosis.
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Cites
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Homocysteine in Health and Disease
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Kontush, A., & Chapman, M. J. (2006) · Pharmacological Reviews · doi:10.1124/pr.58.3.1 · Cited by 647
Costa, L. G., Cole, T. B., Jarvik, G. P., & Furlong, C. E. (2003) · Annual Review of Medicine · doi:10.1146/annurev.med.54.101601.152421 · Cited by 264
Structural Modifications of HDL and Functional Consequences
Ferretti, G., Bacchetti, T., Nègre-Salvayre, A., Salvayre, R., Dousset, N., & Curatola, G. (2006) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2005.08.008 · Cited by 176
Hirche, F., Schröder, A., Knoth, B., Stangl, G. I., & Eder, K. (2006) · British Journal Of Nutrition · doi:10.1079/bjn20061729 · Cited by 68
Metadata
- Authors
- Jakubowski, H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-02
- Volume
- 275
- Issue
- 6
- Pages
- 3957-3962
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2021395497
- Cited by
- 398
- References
- 20
- FWCI
- 10.07
- Type
- journal article
- Language
- en
- Open access
- hybrid
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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.
