Mechanism of cis-prenyltransferase reaction probed by substrate analogues

Biochemical and Biophysical Research Communications

Volumn 400, Issue 4, 2010, Pages 758-762

  Lu, Yen Pin ^a   Liu, Hon Ge ^a   Teng, Kuo Hsun ^b   Liang, Po Huang ^a,b  

^a NATIONAL TAIWAN UNIVERSITY   (Taiwan)

^b INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

Author keywords

Concerted; Isoprenoid; Prenyltransferase; Reaction mechanism; Sequential

Indexed keywords

DIMETHYLALLYLTRANSFERASE; FARNESYL DIPHOSPHATE;

ARTICLE; ENZYME MECHANISM; ENZYME METABOLISM; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; STEADY STATE;

ALKYL AND ARYL TRANSFERASES; CATALYSIS; ESCHERICHIA COLI; HEMITERPENES; ORGANOPHOSPHORUS COMPOUNDS; POLYISOPRENYL PHOSPHATES; SESQUITERPENES; SUBSTRATE SPECIFICITY; TRANSFERASES;

ESCHERICHIA COLI;

EID: 77957260432     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.09.001     Document Type: Article

References (21)

1. Kellogg B.A., Poulter C.D. Chain elongation in the isoprenoid biosynthetic pathway. Cur. Opin. Chem. Biol. 1997, 1:570-578.
2. Ogura K., Koyama T., Sagami H. Polyprenyl diphosphate synthases, subcell. Biochem. 1997, 28:57-87.
3. Liang P.H. Reaction kinetics, catalytic mechanisms, conformational changes, and inhibitor design for prenyltransferases. Biochemistry 2009, 48:6562-6570.
4. Tarshis L.C., Proteau P.J., Kellogg B.A., Sacchettini J.C., Poulter C.D. Regulation of product chain length by isoprenyl diphosphate synthases. Proc. Natl. Acad. Sci. USA 1996, 93:15018-15023.
5. Guo R.T., Kuo C.J., Chou C.C., Ko T.P., Shr H.L., Liang P.H., Wang A.H. Crystal structure of octaprenyl pyrophosphate synthase from hyperthermophilic Thermotoga maritima and mechanism of product chain length determination. J. Biol. Chem. 2004, 279:4903-4912.
6. Hosfield D.J., Zhang Y., Dougan D.R., Broun A., Tari L.W., Swanson R.V., Finn J. Structural basis for bisphosphonate-mediated inhibition of isoprenoid biosynthesis. J. Biol. Chem. 2004, 279:8526-8529.
7. Fujihashi M., Zhang Y.W., Higuchi Y., Li X.Y., Koyama T., Miki K. Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase. Proc. Natl. Acad. Sci. USA 2001, 98:4337-4342.
8. Ko T.P., Chen Y.K., Robinson H., Tsai P.C., Gao Y.G., Chen A.P., Wang A.H., Liang P.H. Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysis. J. Biol. Chem. 2001, 276:47474-47482.
9. Chang S.Y., Ko T.P., Liang P.H., Wang A.H. Catalytic mechanism revealed by the crystal structure of undecaprenyl pyrophosphate synthase in complex with sulfate, magnesium, and triton. J. Biol. Chem. 2003, 278:29298-29307.
10. Guo R.T., Ko T.P., Chen A.P., Kuo C.J., Wang A.H., Liang P.H. Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: roles of the metal ion and conserved residues in catalysis. J. Biol. Chem. 2005, 280:20762-20774.
11. Poulter C.D., Satterwhite D.M. Mechanism of the prenyl-transfer reaction. Studies with (E)- and (Z)-3-trifluoromethyl-2-buten-1-yl pyrophosphate. Biochemistry 1977, 16:5470-5478.
12. Lu Y.P., Liu H.G., Liang P.H. Different reaction mechanisms for cis- and trans-prenyltransferases. Biochem. Biophys. Res. Commun. 2009, 379:351-355.
13. Poulter C.D., Argyle J.C., Mash E.A. Letter: Prenyltransferase. New evidence for an ionization-condensation-elimination mechanism with 2-fluorogeranyl pyrophosphate. J. Am. Chem. Soc. 1977, 99:957-959.
14. Pais J.E., Bowers K.E., Fierke C.A. Measurement of the alpha-secondary isotope effect for the reaction catalyzed by mammalian protein farnesyltransferase. J. Am. Chem. Soc. 2006, 128:15086-15087.
15. Pan J.J., Kuo T.H., Chen Y.K., Yang L.W., Liang P.H. Insight into the catalytic mechanism of Escherichia coli octaprenyl pyrophosphate synthase derived from pre-steady-state kinetic analysis. Biochim. Biophys. Acta 2004, 1594:64-73.
16. Pan J.J., Chiou S.T., Liang P.H. Product distribution and pre-steady-state kinetic analysis of Escherichia coli undecaprenyl pyrophosphate synthase reaction. Biochemistry 2000, 39:10936-10942.
17. Miller D.J., Yu F., Allemann R.K. Aristolochene synthase-catalyzed cyclization of 2-fluorofarnesyl-diphosphate to 2-fluorogermacrene A. Chembiochem 2007, 8:1819-1825.
18. Kim S.H., Heo K., Chang Y.J., Park S.H., Rhee S.K., Kim S.U. Cyclization mechanism of amorpha-4, 11-diene synthase, a key enzyme in artemisinin biosynthesis. J. Nat. Prod. 2006, 69:758-762.
19. Chen A.P.-C., Chen Y.H., Liu H.P., Li Y.C., Chen C.T., Liang P.H. Application of synthetic fluorescent substrate analogues to study ligand interactions for undecaprenyl pyrophosphate synthase. J. Am. Chem. Soc. 2002, 124:15217-15224.
20. Weller V.A., Distefano M.D. Measurement of the α-secondary kinetic isotope effect for a prenyltransferase by MALDI mass spectrometry. J. Am. Chem. Soc. 1998, 120:7975-7976.
21. Chen Y.H., Chen A.P.-C., Chen C.T., Wang A.H.-J., Liang P.H. Probing the conformational change of E. coli undecaprenyl pyrophosphate synthase during catalysis using an inhibitor and tryptophan mutants. J. Biol. Chem. 2002, 277:7369-7376.