Biosynthesis of selenophosphate

BioFactors

Volumn 10, Issue 2-3, 1999, Pages 237-244

  Lacourciere, Gerard M ^a  

^a NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CYSTEINE; PHOSPHATE; SELENIDE; SELENIUM DERIVATIVE; SELENOPROTEIN; SYNTHETASE; THREONINE;

BIOSYNTHESIS; CHEMICAL REACTION; CHEMICAL STRUCTURE; CONFERENCE PAPER; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; HUMAN; HYDROLYSIS; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL;

EID: 0032743146     PISSN: 09516433     EISSN: None     Source Type: Journal    
DOI: 10.1002/biof.5520100222     Document Type: Conference Paper

References (29)

1. W. Leinfelder, K. Forchhammer, F. Zinoni, G. Sawers, M.-A. Mandrand-Berthelot and A. Bock, Escherichia coli genes whose products are involved in selenium metabolism, J. Bacteriol. 170 (1988), 540-546.
2. UCA involvement and characterization of the selD gene product, Proc. Natl. Acad. Sci. USA 87 (1990), 543-547.
3. A. Bock and T.C. Stadtman, Selenocysteine, a highly specific component of certain enzymes, is incorporated by a UGA-directed co-translational mechanism, BioFactors 1 (1988), 245-250.
4. W. Leinfelder, E. Zehelein, M.-A. Mandrand-Berthelot and A. Böck, Genes for a novel tRNA species that accept L-serine and cotranslationally inserts selenocysteine, Nature 331 (1988), 723-725.
5. K. Forchhammer, W. Leinfelder, K. Boesmiller, B. Veprek and A. Böck, Selenocysteine synthase from Escherichia coli. Nucleotide sequence of the gene (selA) and purification of the protein, J. Biol. Chem. 266 (1991), 6318-6323.
6. K. Forchhammer and A. Bock, Selenocysteine synthase from Escherichia coli. Analysis of the reaction sequence, J. Biol. Chem. 266 (1991), 6324-6328.
7. 31P NMR studies show the labile selenium donor synthesized by the selD gene product contains selenium bonded to phosphorous, Proc. Natl. Acad. Sci. USA 89 (1992), 2975-2979.
8. Z. Veres, I.Y. Kim, T.D. Scholz and T.C. Stadtman, Selenophosphate synthetase enzyme properties and catalytic function, J. Biol. Chem. 269 (1994), 10 597-10 603.
9. F. Liu, Q. Dong and H.J. Fromm, Site-directed mutagenesis of the phosphate-binding consensus sequence in Escherichia coli adenylosuccinate synthetase, J. Biol. Chem. 267, 2388-2392.
10. H.R. Bourne, D.A. Sanders and F. McCormick, The GTPase superfamily: conserved structure and molecular mechanism, Nature 349 (1991), 117-127.
11. L.C. Seefeldt, T.V. Morgan, D.R. Dean and L.E. Mortenson, Mapping the site(s) of MgATP and MgADP interaction with the nitrogenase of Azotobacter vinelandii. Lysine 15 of the iron protein plays a major role in MgATP interaction, J. Biol. Chem. 267 (1992), 6680-6688.
12. M. Saraste, P.R. Sibbald and A. Wittinghofer, The P-loop-a common motif in ATP and GTP-binding proteins, Trends Biochem. Sci. 15, 430-434.
13. I.Y. Kim, Z. Veres and T.C. Stadtman, Escherichia coli mutant SELD enzymes, J. Biol. Chem. 267 (1992), 19 650-19 654.
14. 75Se]Selenide, Arch. Biochem. Biophys. 341 (1997), 353-359.
15. L.S. Mullins, S.B. Hong, G.E. Gibson, H. Walker, T.C. Stadtman and F.M. Rauschel, Identification of a phosphorylated enzyme intermediate in the catalytic mechanism for selenophosphate synthetase, J. Am. Chem. Soc. 119 (1997), 6684-6685.
16. H. Walker, J.A. Ferretti and T.C. Stadtman, Isotope exchange studies on the Escherichia coli Selenophosphate synthetase mechanism, Proc. Natl. Acad. Sci. USA 95 (1998), 2180-2185.
17. C.J. Bull, O. White, G.J. Olsen, L. Zhou, R.D. Fleischmann, G.G. Sutton, J.A. Blake, L.M. Fitzgerald, R.A. Clayton, J.D. Gocayne, A.R. Kerlavage, B.A. Dougherty, J.F. Tomb, M.D. Adams, C.I. Reich, R. Overbeek, E.F. Kirkness, K.G. Weinstock, J.M. Merrick, A. Glodek, J.L. Scott, N.S.M. Geoghagen, J.F. Weidman, J.L. Fuhrmann, D. Nguyen, T.R. Utterback, J.M. Kelley, J.D. Peterson, P.W. Sadow, M.C. Hanna, M.D. Cotton, K.M. Roberts, M.A. Hurst, B.P. Kaine, M. Borodovsky, H.P. Klenk, C.M. Fraser, H.O. Smith, C.R. Woese and C.R. Venter, Complete genome sequence of the methanogenic archeon, Methanococcus jannaschii. Science 273 (1996), 1058-1073.
18. R.D. Fleischmann, M.D. Adams, O. White, R.A. Clayton, E.F. Kirkness, A.R. Kerlavage, C.J. Bull, J.F. Tomb, B.A. Dougherty, J.M. Merrick, K. McKenney, G. Sutton, W. Fitzhugh, C.A. Fields, J.D. Gocayne, J.D. Scott, R. Shirley, L.I. Liu, A. Glodek, J.M. Kelley, J.F. Weidman, C.A. Phillips, T. Spriggs, E. Hedblom, M.D. Cotton, T.R. Utterback, M.C. Hanna, D. Nguyen, D.M. Saudek, R.C. Brandon, L.D. Fine, J.L. Fritchman, J.L. Fuhrmann, N.S.M. Geoghagen, C.L. Gnehm, L.A. McDonald, K.V. Small, C.M. Fraser, H.O. Smith, C.J. Venter, Whole-genome random sequencing and assembly of Haemophilus influenzae Rd, Science 269 (1995), 496-512.
19. M.J. Guimaraes, D. Peterson, A. Vicari, B.G. Cocks, N.G. Copeland, D.J. Gilbert, N.A. Jenkins, D.A. Ferrick, R.A. Kastelein, J.F. Bazan and A. Zlotnik, 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, 15 086-15 091.
20. S.C. Low, J.W. Harney and M.J. Berry, Cloning and functional characterization of human selenophosphate synthetase, an essential component of selenoprotein synthesis, J. Biol. Chem. 270 (1995), 21659-21664.
21. B.C. Persson, A. Bock, H. Jackle and G. Vorbruggen, SelD homolog from Drosophila lacking selenide-dependent monoselenophosphate synthetase activity, J. Mol. Biol. 274 (1997), 174-180.
22. R. Wilting, K. Vamvakidou and A. Bock, Functional expression in Escherichia coli of the Haemophilus influenzae gene coding for selenocysteine-containing selenophosphate synthetase, Arch. Microbiol. 169 (1998), 71-75.
23. X. Zhao and D.A. Horne, The role of cysteine residues in the rearrangement of uridine to pseudouridine catalyzed by pseudouridine synthase I, J. Biol. Chem. 272 (1997), 1950-1955.
24. T.C. Stadtman, G.L. Dilworth and C.S. Chen, Selenium dependent bacterial enzymes, in: Proceedings or the Third International Symposium on Organic Selenium and Tellurium Compounds, D. Cagniant and G. Kirsch, eds, 1979, pp. 115-130.
25. N. Esaki, T. Nakamura, H. Tanaka and K. Soda, Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine, J. Biol. Chem. 275 (1982), 4386-4391.
26. P. Chocat, N. Esaki, K. Tanizawa, K. Nakamura, H. Tanaka and K. Soda, Purification and characterization of selenocysteine β-lyase from Citrobacter freundii, J. Bacteriol. 163 (1985), 669-676.
27. H. Mihara, T. Kurihara, T. Yoshimura, K. Soda and N. Esaki, Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities, J. Biol. Chem. 272 (1997), 22 417-22 424.
28. L. Zheng, R.H. White, V.L. Cash, R.F. Jack and D.R. Dean, Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis, Proc. Natl. Sci. USA 90, 2754-2758.
29. L. Zheng, R.H. White, V.L. Cash and D.R. Dean, Mechanism for the desulfurization of L-cysteine catalyzed by the nifs gene product, Biochemistry 33 (1994), 4714-4720.