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Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme.
Open accessAbstract
We have found a novel enzyme that exclusively decomposes L-selenocysteine into L-alanine and H2Se in various mammalian tissues, and have named it selenocysteine lyase. The enzyme from pig liver has been purified to homogeneity. It has a molecular weight of approximately 85,000, and contains pyridoxal 5'-phosphate as a coenzyme. Its maximum reactivity is at about pH 9.0. Balance studies showed that 1 mol of selenocysteine is converted to equimolar amounts of alanine and H2Se. The following amino acids are insert: L-cysteine, L-serine, L-cysteine sulfinate, selenocysteamine, Se-ethyl-DL-selenocysteine, and L-selenohomocysteine. L-Cysteine (Ki, 1.0 mM) competes with L-selenocysteine (Km, 0.83 mM) to inhibit the enzyme reaction. The enzyme is the first proven enzyme that specifically acts on selenium compounds.
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Cited by
Terry, N., Zayed, A. M., de Souza, M. P., & Tarun, A. S. (2000) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.arplant.51.1.401 · Cited by 1,328
Regulation of Selenium Metabolism and Transport
Burk, R. F., & Hill, K. E. (2015) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071714-034250 · Cited by 658
Selenium metabolism and bioavailability
Daniels, L. A. (1996) · Biological Trace Element Research · doi:10.1007/bf02784430 · Cited by 306
Arsenic–selenium and mercury–selenium bonds in biology
GAILER, J. (2007) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2006.07.018 · Cited by 180
Overexpression of AtCpNifS Enhances Selenium Tolerance and Accumulation in Arabidopsis
Van Hoewyk, D., Garifullina, G. F., Ackley, A. R., Abdel-Ghany, S. E., Marcus, M. A., Fakra, S., Ishiyama, K., Inoue, E., Pilon, M., Takahashi, H., et al. (2005) · Plant Physiology · doi:10.1104/pp.105.068684 · Cited by 151
Metadata
- Authors
- Esaki, N., Nakamura, T., Tanaka, H., & Soda, K.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1982-04
- Volume
- 257
- Issue
- 8
- Pages
- 4386-4391
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1550873995
- Cited by
- 237
- References
- 0
- FWCI
- 6.11
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme. https://app.cochat.ai/papers/10.1016/s0021-9258(18)34734-3
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- Esaki, N., Nakamura, T., Tanaka, H., & Soda, K. (1982). Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)34734-3
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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.
