Reaction kinetic pathway of the recombinant octaprenyl pyrophosphate synthase from Thermotoga maritima: How is it different from that of the mesophilic enzyme

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1599, Issue 1-2, 2002, Pages 125-133

  Kuo, Tun Hsun ^a   Liang, Po Huang ^a,b  

^a NATIONAL TAIWAN UNIVERSITY   (Taiwan)

^b INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

Author keywords

Mesophile; Prenyltransferase; Single turnover; Thermophile; Ubiquinone

Indexed keywords

BACTERIAL ENZYME; FARNESYL DIPHOSPHATE; OCTAPRENYL PYROPHOSPHATE SYNTHASE; RECOMBINANT ENZYME; SYNTHETASE; UNCLASSIFIED DRUG; HEPTAPRENYLTRANSFERASE; TRANSFERASE;

ANAEROBIC BACTERIUM; ARTICLE; BACTERIAL GENETICS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME STRUCTURE; ESCHERICHIA COLI; GENETIC CODE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN POLYMERIZATION; SPECIES COMPARISON; STEADY STATE; TEMPERATURE DEPENDENCE; THERMOPHILIC BACTERIUM; THERMOSTABILITY; THERMOTOGA MARITIMA; AMINO ACID SEQUENCE; CHEMISTRY; ENZYMOLOGY; KINETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; TEMPERATURE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; THERMOTOGA; THERMOTOGA MARITIMA;

ALKYL AND ARYL TRANSFERASES; AMINO ACID SEQUENCE; KINETICS; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; TEMPERATURE; THERMOTOGA MARITIMA;

EID: 0037163391     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(02)00410-7     Document Type: Article

References (28)

1. Adams M.W.W. Enzymes and proteins from organisms that grow near and above 100 degrees Celsius. Annu. Rev. Microbiol. 47:1993;627-658.
2. Day M.W., Hsu B.T., Joshua-Tor L., Park J.B., Zhou Z.H., Adams M.W., Rees D.C. X-ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium Pyrococcus furiosus. Protein Sci. 1:1992;1494-1507.
3. Huber R., Langworthy T.A., Konig H., Thomm M., Woese C.R., Sleytr U.B., Stetter K.O. Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90 °C. Arch. Microbiol. 144:1986;324-333.
4. Ogura K., Koyama T., Sagami H. Polyprenyl diphosphate synthases. Sub-cell. Biochem. 28:1997;57-87. (Chapter 3).
5. Ogura K., Koyama T. Enzymatic aspects of isoprenoid chain elongation. Chem. Rev. 98:1998;1263-1276.
6. Fujisaki S., Nishino T., Katsuki H. Isoprenoid synthesis in Escherichia coli. Separation and partial purification of four enzymes involved in the synthesis. J. Biochem. 99:1986;1327-1337.
7. Asai K.-I., Fujisaki S., Nishimura Y., Nishino T., Okada K., Nakagawa T., Kawamukai M., Matsuda H. The identification of Escherichia coli ispB (cel) gene encoding the octaprenyl diphosphate synthase. Biochem. Biophys. Res. Commun. 202:1994;340-345.
8. Okada K., Suzuki K., Kamiya Y., Zhu X., Fujisaki S., Nishimura Y., Nishino T., Nakagawa T., Kawamukai M., Matsuda H. Polyprenyl diphosphate synthase essentially defines the length of the side chain of ubiquinone. Biochim. Biophys. Acta. 1302:1996;217-223.
9. Okada K., Minehira M., Zhu X., Suzuki K., Nakagawa T., Matsuda H., Kawamukai M. The ispB gene encoding octaprenyl diphosphate synthase is essential for growth of Escherichia coli. J. Bacteriol. 179:1997;3058-3060.
10. Collin M.D., Jones D. Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implication. Microbiol. Rev. 45:1981;316-354.
11. Ashby M.N., Edwards P.A. Elucidation of the deficiency in two yeast coenzyme Q mutants. Characterization of the structural gene encoding hexaprenyl pyrophosphate synthetase. J. Biol. Chem. 265:1990;13157-13164.
12. Teclebrhan H., Olsson J., Swiezewska E., Dallner G. Biosynthesis of the side chain of ubiquinone:trans-prenyltransferase in rat liver microsomes. J. Biol. Chem. 268:1993;23081-23086.
13. Ernster L., Dallner G. Biochemical, physiological and medical aspects of ubiquinone function. Biochim. Biophys. Acta. 1271:1995;195-204.
14. Pan J.J., Kuo T.H., Chen Y.K., Yang L.W., Liang P.H. Insight into the activation mechanism of E. coli octaprenyl pyrophosphate synthase derived from pre-steady-state kinetic analysis. Biochim. Biophys. Acta. 1594:2002;64-73.
15. Liang P.H., Ko T.P., Wang A.H.-J. Structure, mechanism and function of prenyltransferases. Eur. J. Biochem. 269:2002;3339-3354. (doi:10.1046/j.1432- 1033.2002.03014.x)).
16. Fujii H., Koyama T., Ogura K. Efficient enzymatic hydrolysis of polyprenyl pyrophosphate. Biochim. Biophys. Acta. 712:1982;716-718.
17. Shimizu N., Koyama T., Ogura K. Molecular cloning, expression, and purification of undecaprenyl diphosphate synthase. J. Biol. Chem. 273:1998;19476-19481.
18. Barshop B.A., Wrenn R.F., Frieden C. Analysis of numerical methods for computer simulation of kinetic processes: development of KINSIM - a flexible, portable system. Anal. Biochem. 130:1983;134-145.
19. Davison P.F. Proteins in denaturing solvents: gel exclusion studies. Science. 161:1968;906-907.
20. Sreerama N., Woody R.W. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 209:1993;32-44.
21. Eftink M.R. Use of multiple spectroscopic methods to monitor equilibrium unfolding of proteins. Methods Enzymol. 259:1995;487-512.
22. Pan J.J., Chiu S.T., Liang P.H. Product distribution and pre-steady-state kinetic analysis of E. coli undecaprenyl pyrophosphate synthase. Biochemistry. 39:2000;10936-10942.
23. Pan J.J., Yang L.W., Liang P.H. Effect of site-directed mutagenesis of the conserved aspartate and glutamate on E. coli undecaprenyl pyrophosphate synthase catalysis. Biochemistry. 39:2000;13856-13861.
24. Ko T.P., Chen Y.K., Robinson H., Tsai P.C., Gao Y.G., Chen A.P.-C., Wang A.H.-J., Liang P.H. Mechanism of the product chain length determination and the role of a flexible loop in undecaprenyl pyrophosphate synthase catalysis. J. Biol. Chem. 276:2001;47474-47486.
25. Kainou T., Okada K., Suzuki K., Nakagawa T., Matsuda H., Kawamukai M. Dimer formation of octaprenyl-diphosphate synthase (IspB) is essential for chain length determination of ubiquinone. J. Biol. Chem. 276:2001;7876-7883.
26. Altschul S.F., Madden T.L., Schaffer A.A., Zhang J., Zhang Z., Miller W., Lipman D.J. Gapped BLAST and PSI-BLAST: a new generation of protein database search program. Nucleic Acids Res. 25:1997;3389-3402.
27. Soballe B., Poole R.K. Microbial ubiquinones: multiple roles in respiration, gene regulation and oxidative stress management. Microbiology. 145:1999;1817-1830.
28. Chen Y.H., Chen A.P.-C., Chen C.T., Wang A.H.-J., Liang P.H. Probing the conformational change of Escherichia coli undecaprenyl pyrophosphate synthase during catalysis using an inhibitor and tryptophan mutants. J. Biol. Chem. 277:2002;7369-7376.