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EcoSal Plus

Domain 3:

Metabolism

Selenocysteine Lyase

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  • Author: Thressa C. Stadtman1
  • Editor: Valley Stewart2
  • VIEW AFFILIATIONS HIDE AFFILIATIONS
    Affiliations: 1: Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Building 50, Room 2120, Bethesda, MD 20892-8012; 2: University of California, Davis, Davis, CA
  • Received 04 February 2004 Accepted 06 April 2004 Published 27 July 2004
  • Address correspondence to Thressa C. Stadtman tcstadtman@nih.gov
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  • Abstract:

    Selenocysteine is a naturally occurring analog of cysteine in which the sulfur atom of the latter is replaced with selenium. This seleno-amino acid occurs as a specific component of various selenoproteins and selenium-dependent enzymes. Incorporation of selenocysteine into these proteins occurs cotranslationally as directed by the UGA codon. For this process, a special tRNA having an anticodon complimentary to UGA, tRNA, is utilized. In and related bacteria, this tRNA first is amino acylated with serine, and the seryl-tRNA is converted to selenocysteyl-tRNA. The specific incorporation of selenocysteine into proteins directed by the UGA codon depends on the synthesis of selenocysteyl-tRNA. Included in the selenium delivery protein category are rhodaneses that mobilize selenium from inorganic sources and NIFS-like proteins that liberate elemental selenium from selenocysteine. The NIFS protein from was found to serve as an efficient catalyst in vitro for delivery of selenium from free selenocysteine to selenophosphate synthetase for selenophosphate formation. The widespread distribution of selenocysteine lyase in numerous bacterial species was reported and the bacterial enzymes, like the pig liver enzyme, required pyridoxal phosphate as cofactor. Three NIFS-like genes were isolated from by Esaki and coworkers and the expressed gene products were isolated and characterized. One of these NIFS-like proteins also exhibited a high preference for selenocysteine over cysteine. , an anaerobic methane-producing organism, that grows in a mineral medium containing formate as sole organic carbon source, synthesizes several specific selenoenzymes required for growth and energy production under these conditions.

  • Citation: Stadtman T. 2004. Selenocysteine Lyase, EcoSal Plus 2004; doi:10.1128/ecosalplus.3.6.1.1.1

Key Concept Ranking

Amino Acids
0.63890225
Selenocysteine Lyase
0.59640163
Proteins
0.5587361
Escherichia coli
0.52185136
0.63890225

References

1. Bőck A, Thanbichler M. July 2004, posting date. Selenocysteine, Selenocysteine. In R. Curtiss III (Editor in Chief), EcoSal—Escherichia coli and Salmonella: Cellular and Molecular Biology. [Online.] http://www.ecosal.org. ASM Press, Washington, D.C.
2. Ehrenreich A, Forchhammer K, Tormay P, Veprek B, Bőck A. 1992. Selenoprotein synthesis in E. coli: purification and characterization of the enzyme catalyzing selenium activation. Eur J Biochem 206:767–773. [PubMed][CrossRef]
3. Glass RS, Singh WP, Jung W, Veres Z, Scholz TD, Stadtman TC. 1993. Monoselenophosphate: synthesis, characterization, and identity with the prokaryotic biological selenium donor compound, SePX. Biochemistry 32:12555–12559. [PubMed][CrossRef]
4. Veres Z, Kim IY, Scholz TD, Stadtman TC. 1994. Selenophosphate synthetase: enzyme properties and catalytic reaction. J Biol Chem 269:10597–10603.[PubMed]
5. Veres Z, Tsai L, Scholz TD, Politino M, Balaban RS, Stadtman TC. 1992. Synthesis of 5-methyl-aminomethyl-2-selenouridine in tRNAs: 31P NMR studies show the labile selenium donor synthesized by the selD gene product contains selenium bonded to phosphorus. Proc Natl Acad Sci USA 89:2975–2979. [CrossRef]
6. Flint DH. 1996. Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the NIFS gene of Azotobacter vinelandii and that can participate in the synthesis of the FeS cluster of dihydroxy acid dehydratase. J Biol Chem 271:16068–16074.[PubMed]
7. Zeng L, White RH, Cash VL, Dean DR. 1994. Mechanism for the desulfurization of L-cysteine catalyzed by the NIFS gene product. Biochemistry 33:4714–4720. [PubMed][CrossRef]
8. Zeng L, White RH, Cash VL, Jack RF, Dean DR. 1993. Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis. Proc Natl Acad Sci USA 90:2754–2758. [PubMed][CrossRef]
9. Lacourciere GM, Stadtman TC. 1998. The NIFS protein can function as a selenide delivery protein in the biosynthesis of selenophosphate. J Biol Chem 273:30921–30926. [PubMed][CrossRef]
10. Lacourciere GM, Mihara H, Kurihara T, Esaki N, Stadtman TC. 2000. Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate. J Biol Chem 275:23769–23773. [CrossRef]
11. Lacourciere GM. 2002. Selenium is mobilized in vivo from free selenocysteine and is incorporated specifically into formate dehydrogenase H and tRNA nucleosides. J Bacteriol 184:1940–1946. [PubMed][CrossRef]
12. 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. J Biol Chem 257:4386–4391.[PubMed]
13. Chocat P, Esaki N, Nakamura T, Tanaka H, Soda K. 1983. Microbial distribution of selenocysteine lyase. J Bacteriol 156:455–457. [PubMed]
14. Chocat P, Esaki N, Tanizawa K, Nakamura K, Tanaka H, Soda K. 1985. Purification and characterization of selenocysteine β-lyase from Citrobacter freundii. J Bacteriol 163:669–676.[PubMed]
15. Mihara H, Kurihara T, Watanabe T, Yoshimura T, Esaki N. 2000. cDNA cloning, purification, and characterization of mouse liver selenocysteine lyase. Candidate for selenium delivery protein in selenoprotein synthesis. J Biol Chem 275:6195–6200. [PubMed][CrossRef]
16. Mihara H, Kurihara T, Yoshimura T, Soda K, Esaki N. 1997. Cysteine desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities: gene cloning, purification, and characterization of a novel pyridoxal enzyme. J Biol Chem 272:22417–22424. [PubMed][CrossRef]
17. Mihara H, Maeda M, Fujii T, Kurihara T, Hata Y, Esaki N. 1999. The NIFS-like gene, csd-B, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase: gene cloning, purification, characterization, and preliminary X-ray crystallographic studies. J Biol Chem 274:14768–4772. [PubMed][CrossRef]
18. Mihara H, Kurihara T, Yoshimura T, Esaki N. 2000. Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic differences between L-cysteine desulfurase and L-selenocysteine lyase reactions. J Biochem 127:559–567.
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/content/journal/ecosalplus/10.1128/ecosalplus.3.6.1.1.1
2004-07-27
2017-05-29

Abstract:

Selenocysteine is a naturally occurring analog of cysteine in which the sulfur atom of the latter is replaced with selenium. This seleno-amino acid occurs as a specific component of various selenoproteins and selenium-dependent enzymes. Incorporation of selenocysteine into these proteins occurs cotranslationally as directed by the UGA codon. For this process, a special tRNA having an anticodon complimentary to UGA, tRNA, is utilized. In and related bacteria, this tRNA first is amino acylated with serine, and the seryl-tRNA is converted to selenocysteyl-tRNA. The specific incorporation of selenocysteine into proteins directed by the UGA codon depends on the synthesis of selenocysteyl-tRNA. Included in the selenium delivery protein category are rhodaneses that mobilize selenium from inorganic sources and NIFS-like proteins that liberate elemental selenium from selenocysteine. The NIFS protein from was found to serve as an efficient catalyst in vitro for delivery of selenium from free selenocysteine to selenophosphate synthetase for selenophosphate formation. The widespread distribution of selenocysteine lyase in numerous bacterial species was reported and the bacterial enzymes, like the pig liver enzyme, required pyridoxal phosphate as cofactor. Three NIFS-like genes were isolated from by Esaki and coworkers and the expressed gene products were isolated and characterized. One of these NIFS-like proteins also exhibited a high preference for selenocysteine over cysteine. , an anaerobic methane-producing organism, that grows in a mineral medium containing formate as sole organic carbon source, synthesizes several specific selenoenzymes required for growth and energy production under these conditions.

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