Cloning and functional analysis of novel short-chain cis-prenyltransferases

Biochemical and Biophysical Research Communications

Volumn 375, Issue 4, 2008, Pages 536-540

  Ambo, Takanori ^a   Noike, Motoyoshi ^a   Kurokawa, Hirofumi ^a   Koyama, Tanetoshi ^a  

^a TOHOKU UNIVERSITY   (Japan)

Author keywords

Chain length determination; cis Farnesyl diphosphate synthase; Prenyltransferase; Substrate specificity

Indexed keywords

DIMETHYLALLYLTRANSFERASE; ISOLEUCINE;

ARTICLE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME LOCALIZATION; ENZYME MECHANISM; ENZYME REGULATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; MOLECULAR CLONING; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN SYNTHESIS; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS;

ACTINOMYCETALES; BACTERIAL PROTEINS; CATALYSIS; CLONING, MOLECULAR; CORYNEBACTERIUM GLUTAMICUM; ISOLEUCINE; MUTAGENESIS, SITE-DIRECTED; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY; TRANSFERASES;

MYCOBACTERIUM TUBERCULOSIS;

EID: 51449089205     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.08.057     Document Type: Article

References (26)

1. Ogura K., and Koyama T. Enzymatic aspects of isoprenoid chain elongation. Chem. Rev. 98 (1998) 1263-1276
2. Wang K.C., and Ohnuma S. Isoprenyl diphosphate synthases. Biochim. Biophys. Acta 1529 (2000) 33-48
3. Kellogg B.A., and Poulter C.D. Chain elongation in the isoprenoid biosynthetic pathway. Curr. Opin. Chem. Biol. 1 (1997) 570-578
4. Kharel Y., and Koyama T. Molecular analysis of cis-prenyl chain elongating enzymes. Nat. Prod. Rep. 20 (2003) 111-118
5. Ohnuma S., Narita K., Nakazawa T., Ishida C., Takeuchi Y., Ohto C., and Nishino T. A role of the amino acid residue located on the fifth position before the first aspartate-rich motif of farnesyl diphosphate synthase on determination of the final product. J. Biol. Chem. 271 (1996) 30748-30754
6. Wang K., and Ohnuma S. Chain-length determination mechanism of isoprenyl diphosphate synthases and implications for molecular evolution. Trends Biochem. Sci. 24 (1999) 445-451
7. Tarshis L.C., Proteau P.J., Kellogg B.A., Sacchettini J.C., and Poulter C.D. Regulation of product chain length by isoprenyl diphosphate synthases. Proc. Natl. Acad. Sci. USA 93 (1996) 15018-15023
8. Shimizu N., Koyama T., and Ogura K. Molecular cloning, expression, and purification of undecaprenyl diphosphate synthase. No sequence similarity between E- and Z-prenyl diphosphate synthases. J. Biol. Chem. 273 (1998) 19476-19481
9. Fujihashi M., Zhang Y.W., Higuchi Y., Li X.Y., Koyama T., and Miki K. Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase. Proc. Natl. Acad. Sci. USA 98 (2001) 4337-4342
10. Fujikura K., Zhang Y.W., Yoshizaki H., Nishino T., and Koyama T. Significance of Asn-77 and Trp-78 in the catalytic function of undecaprenyl diphosphate synthase of Micrococcus luteus B-P 26. J. Biochem. (Tokyo) 128 (2000) 917-922
11. Fujikura K., Zhang Y.W., Fujihashi M., Miki K., and Koyama T. Mutational analysis of allylic substrate binding site of Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase. Biochemistry 42 (2003) 4035-4041
12. Kharel Y., Zhang Y.W., Fujihashi M., Miki K., and Koyama T. Identification of significant residues for homoallylic substrate binding of Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase. J. Biol. Chem. 276 (2001) 28459-28464
13. Tarshis L.C., Yan M., Poulter C.D., and Sacchettini J.C. Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-Å resolution. Biochemistry 33 (1994) 10871-10877
14. Apfel C.M., Takacs B., Fountoulakis M., Stieger M., and Keck W. Use of genomics to identify bacterial undecaprenyl pyrophosphate synthetase: cloning, expression, and characterization of the essential uppS gene. J. Bacteriol. 181 (1999) 483-492
15. Sato M., Sato K., Nishikawa S., Hirata A., Kato J., and Nakano A. The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis. Mol. Cell Biol. 19 (1999) 471-483
16. Sato M., Fujisaki S., Sato K., Nishimura Y., and Nakano A. Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis. Genes Cells 6 (2001) 495-506
17. Oh S.K., Han K.H., Ryu S.B., and Kang H. Molecular cloning, expression, and functional analysis of a cis-prenyltransferase from Arabidopsis thaliana. Implications in rubber biosynthesis. J. Biol. Chem. 275 (2000) 18482-18488
18. Cunillera N., Arro M., Fores O., Manzano D., and Ferrer A. Characterization of dehydrodolichyl diphosphate synthase of Arabidopsis thaliana, a key enzyme in dolichol biosynthesis. FEBS Lett. 477 (2000) 170-174
19. 50) chain isoprenyl diphosphate synthase in Mycobacterium tuberculosis. J. Biol. Chem. 275 (2000) 22876-22881
20. Asawatreratanakul K., Zhang Y.W., Wititsuwannakul D., Wititsuwannakul R., Takahashi S., Rattanapittayaporn A., and Koyama T. Molecular cloning, expression and characterization of cDNA encoding cis-prenyltransferases from Hevea brasiliensis. A key factor participating in natural rubber biosynthesis. Eur. J. Biochem. 270 (2003) 4671-4680
21. Kharel Y., Takahashi S., Yamashita S., and Koyama T. Manipulation of prenyl chain length determination mechanism of cis-prenyltransferases. FEBS J. 273 (2006) 647-657
22. Schulbach M.C., Mahapatra S., Macchia M., Barontini S., Papi C., Minutolo F., Bertini S., Brennan P.J., and Crick D.C. Purification, enzymatic characterization, and inhibition of the Z-farnesyl diphosphate synthase from Mycobacterium tuberculosis. J. Biol. Chem. 276 (2001) 11624-11630
23. Davisson V.J., Woodside A.B., and Poulter C.D. Synthesis of allylic and homoallylic isoprenoid pyrophosphates. Methods Enzymol. 110 (1985) 130-144
24. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
25. Fujii H., Koyama T., and Ogura K. Efficient enzymatic hydrolysis of polyprenyl pyrophosphates. Biochim. Biophys. Acta 712 (1982) 716-718
26. Chang S.Y., Ko T.P., Chen A.P.C., Wang A.H.J., and Liang P.H. Substrate binding mode and reaction mechanism of undecaprenyl pyrophosphate synthase deduced from crystallographic studies. Protein Sci. 13 (2004) 971-978