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EcoSal Plus

Domain 3:

Metabolism

Selenophosphate Synthetase

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  • Author: Matt D. Wolfe1
  • 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 2122, Bethesda, MD 20892-8012; 2: University of California, Davis, Davis, CA
  • Received 19 November 2003 Accepted 28 January 2004 Published 06 July 2004
  • Address correspondence to Matt D. Wolfe wolfem@nhlbi.nih.gov
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  • Abstract:

    Selenophosphate synthetase, the gene product from , is one of the enzymes required for the synthesis and specific insertion of selenocysteine into proteins directed by the TGA codon. Selenophosphate synthetases have been isolated from or are thought to be present in most organisms; however, the best characterized selenophosphate synthetase is from , in which both in vivo and in vitro studies have been performed. Leinfelder and coworkers showed that an mutant lacking an intact gene fails to incorporate Se into both the selenocysteine-containing enzyme formate dehydrogenase (FDH) and tRNA species that normally contain 2-selenouridine residues at the wobble position. Thus, this study strongly implicated selenophosphate as playing a major role in selenium metabolic pathways. The selenophosphate synthetase reaction requires some form of reduced selenium such as hydrogen selenide (HSe) and ATP as substrates to generate a stoichiometric amount of SePO, AMP, and orthophosphate. Studies of selenophosphate inhibition have provided further insight into the mechanism of selenophosphate synthetase. An assay by which AMP formation is measured in the absence of selenide showed that selenophosphate synthetase catalyzes hydrolysis of ATP to AMP and two orthophosphates in an uncoupled reaction. The sequencing of selenophosphate synthetase genes from various organisms reveals several conserved regions in the gene product. Recent investigations into the mechanism of selenophosphate synthetase have revealed a property of selenophosphate synthetase not previously observed. In samples of purified selenophosphate synthetase, an unusual optical absorption spectrum is seen.

  • Citation: Wolfe M. 2004. Selenophosphate Synthetase, EcoSal Plus 2004; doi:10.1128/ecosalplus.3.6.1.1.2

Key Concept Ranking

Nuclear Magnetic Resonance Spectroscopy
0.46891212
Aromatic Amino Acids
0.3423117
0.46891212

References

1. Stadtman TC. 1996. Selenocysteine. Annu Rev Biochem 65:83–100. [PubMed][CrossRef]
2. Veres Z, Tsai L, Scholz TD, Politino M, Balaban RS, Stadtman TC. 1992. Synthesis of 5-methylaminomethyl-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. [PubMed][CrossRef]
3. Guimaraes MJ, Peterson D, Vicari A, Cocks BG, Copeland NG, Gilbert DJ, Jenkins NA, Ferrick DA, Kastelein RA, Bazan JF, Zlotnik A. 1996. Identification of a novel selD homolog from Eukaryotes, Bacteria, and Archaea: is there an autoregulatory mechanism in selenocysteine metabolism? Proc. Natl Acad Sci USA 93:15086–15091. [CrossRef]
4. Leinfelder W, Forchhammer K, Veprek B, Zehelein E, Böck A. 1990. In vitro synthesis of selenocysteinyl-tRNAUCA from seryl-tRNAUCA: involvement and characterization of the selD gene product. Proc Natl Acad Sci USA 87:543–547. [PubMed][CrossRef]
5. Veres Z, Kim IY, Scholz TD, Stadtman TC. 1994. Selenophosphate synthetase: enzyme properties and catalytic reaction. J Biol Chem 269:10597–10603. [PubMed]
6. 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]
7. 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]
8. Kim IY, Veres Z, Stadtman TC. 1993. Biochemical analysis of Escherichia coli selenophosphate synthetase mutants: lysine 20 is essential for catalytic activity and cysteine 17/19 for 8-azido-ATP derivatization. J Biol Chem 268:27020–27025. [PubMed]
9. Kim IY, Stadtman TC. 1994. Effects of monovalent cations and divalent metal ions on Escherichia coli selenophosphate synthetase. Proc Natl Acad Sci USA 91:7326–7329. [PubMed][CrossRef]
10. Ehrenreich A, Forschhammer K, Tormay P, Veprek B, Böck A. 1992. Selenoprotein synthesis in E. coli: purification and characterization of the enzyme catalyzing selenium activation Eur J Biochem 206:767–773. [PubMed][CrossRef]
11. 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]
12. Liu SY, Stadtman TC. 1997. Selenophosphate synthetase: enzyme labeling studies with [γ-32P]ATP, [β-32P]ATP, [8-14C]ATP, and [75Se]selenide. Arch Biochem Biophys 341:353–359. [PubMed][CrossRef]
13. Evans HJ, Wood HG. 1968. The mechanism of the pyruvate, phosphate dikinase reaction. Proc Natl Acad Sci USA 61:1448–1453. [PubMed][CrossRef]
14. Mullins LS, Hong SB, Gibson GE, Walker H, Stadtman TC, Raushel FM. 1997. Identification of a phosphorylated enzyme intermediate in the catalytic mechanism for selenophosphate synthetase. J Am Chem Soc 119:6684–6685. [CrossRef]
15. Walker H, Ferretti JA, Stadtman TC. 1998. Isotope exchange studies on the Escherichia coli selenophosphate synthetase mechanism. Proc Natl Acad Sci USA 95:2180–2185. [PubMed][CrossRef]
16. Kim IY, Veres Z, Stadtman TC. 1992. Escherichia coli mutant SELD enzymes: the cysteine 17 residue is essential for selenophosphate formation from ATP and selenide. J Biol Chem 267:19650–19654. [PubMed]
17. Wolfe MD. 2003. Mechanistic insights revealed through characterization of a novel chromophore in selenophosphate synthetase from Escherichia coli. IUBMB Life 55:689–693. [PubMed][CrossRef]
18. Axley MJ, Böck A, Stadtman TC. 1991. Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium. Proc Natl Acad Sci USA 88:8450–8454. [PubMed][CrossRef]
19. Lee S-R, Bar-Noy S, Kwon J, Levine RL, Stadtman TC, Rhee SG. 2000. Mammalian thioredoxin reductase: oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity. Proc Natl Acad Sci USA 97:2521–2526. [PubMed][CrossRef]
20. Lacourciere GM, Stadtman TC. 1999. Catalytic properties of selenophosphate synthetases: comparison of the selenocysteine-containing enzyme from Haemophilus influenzae with the corresponding cysteine-containing enzyme from Escherichia coli. Proc Natl Acad Sci USA 96:44–48. [PubMed][CrossRef]
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/content/journal/ecosalplus/10.1128/ecosalplus.3.6.1.1.2
2004-07-06
2017-05-29

Abstract:

Selenophosphate synthetase, the gene product from , is one of the enzymes required for the synthesis and specific insertion of selenocysteine into proteins directed by the TGA codon. Selenophosphate synthetases have been isolated from or are thought to be present in most organisms; however, the best characterized selenophosphate synthetase is from , in which both in vivo and in vitro studies have been performed. Leinfelder and coworkers showed that an mutant lacking an intact gene fails to incorporate Se into both the selenocysteine-containing enzyme formate dehydrogenase (FDH) and tRNA species that normally contain 2-selenouridine residues at the wobble position. Thus, this study strongly implicated selenophosphate as playing a major role in selenium metabolic pathways. The selenophosphate synthetase reaction requires some form of reduced selenium such as hydrogen selenide (HSe) and ATP as substrates to generate a stoichiometric amount of SePO, AMP, and orthophosphate. Studies of selenophosphate inhibition have provided further insight into the mechanism of selenophosphate synthetase. An assay by which AMP formation is measured in the absence of selenide showed that selenophosphate synthetase catalyzes hydrolysis of ATP to AMP and two orthophosphates in an uncoupled reaction. The sequencing of selenophosphate synthetase genes from various organisms reveals several conserved regions in the gene product. Recent investigations into the mechanism of selenophosphate synthetase have revealed a property of selenophosphate synthetase not previously observed. In samples of purified selenophosphate synthetase, an unusual optical absorption spectrum is seen.

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Figures

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Figure 1

Citation: Wolfe M. 2004. Selenophosphate Synthetase, EcoSal Plus 2004; doi:10.1128/ecosalplus.3.6.1.1.2
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Image of Figure 2
Figure 2

An unidentified nucleophilic residue (X) on selenophosphate synthetase would react with the γ-phosphoryl group of ATP. Nucleophilic attack by selenide to form SePO and hydrolysis of ADP would follow to complete the reaction.

Citation: Wolfe M. 2004. Selenophosphate Synthetase, EcoSal Plus 2004; doi:10.1128/ecosalplus.3.6.1.1.2
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Image of Figure 3
Figure 3

Nucleotide binding motifs A and B are boxed, and residues of the selenophosphate synthetase that have been mutated and the resulting enzymes studied are indicated with (?). U indicates selenocysteine. Organisms listed: D.m., ; H.s., ; M.m., ; H.i., ; E.c., ; M.j., .

Citation: Wolfe M. 2004. Selenophosphate Synthetase, EcoSal Plus 2004; doi:10.1128/ecosalplus.3.6.1.1.2
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Image of Figure 4
Figure 4

(A) UV/visible (UV/Vis) spectrum of purified enzyme. The inset is an enlargement showing the region of the chromophore. (B) UV/Vis spectra of the chromophore in the absence (solid line) and presence (dotted line) of Mg/ATP and 20 mM KCl. The inset is a difference spectrum of the Mg/ATP-bound and -unbound forms of selenophosphate synthetase.

Citation: Wolfe M. 2004. Selenophosphate Synthetase, EcoSal Plus 2004; doi:10.1128/ecosalplus.3.6.1.1.2
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Tables

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Table 1

Some properties of wild-type and various mutants of selenophosphate synthetase

Citation: Wolfe M. 2004. Selenophosphate Synthetase, EcoSal Plus 2004; doi:10.1128/ecosalplus.3.6.1.1.2

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