Catalytic function of the residues of phenylalanine and tyrosine conserved in squalene-hopene cyclases

Bioscience, Biotechnology and Biochemistry

Volumn 65, Issue 10, 2001, Pages 2233-2242

  Sato, Tsutomu ^a   Hoshino, Tsutomu ^a  

^a NIIGATA UNIVERSITY   (Japan)

Author keywords

Alicyclobacillus acidocaldarius; Hopene; Squalene; Terpene cyclase; Triterpene

Indexed keywords

ALICYCLOBACILLUS ACIDOCALDARIUS;

MUTASE; PHENYLALANINE; SQUALENE HOPENE CYCLASE; SQUALENE-HOPENE CYCLASE; TYROSINE;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; DNA SEQUENCE; ENDOSPORE-FORMING RODS AND COCCI; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MOLECULAR GENETICS; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; BINDING SITES; CATALYSIS; GRAM-POSITIVE ENDOSPORE-FORMING RODS; INTRAMOLECULAR TRANSFERASES; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHENYLALANINE; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID; SUPPORT, NON-U.S. GOV'T; TYROSINE;

EID: 0035489578     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.65.2233     Document Type: Article

References (27)

1. Abe, I., Rohmer, M., and Prestwich, G. D., Enzymatic cyclization of squalene and oxidosqualene to sterols and triterpenes. Chem. Rev., 93, 2189-2206 (1993).
2. Wendt, K. U., Schulz, G. E., Corey, E. J., and Liu, D. R., Enzyme mechanisms for polycyclic triterpene formation. Angew. Chem. Int. Ed., 39, 2812-2833 (2000).
3. Hoshino, T., Insight into the active sites of squalene cyclase and the cyclization mechanism (in Japanese). Bioscience & Industry, 59, 167-170 (2001).
4. Sato, T., Abe, T., and Hoshino, T., On the cyclization mechanism of squalene: a ring expansion process of the five-membered D-ring intermediate. J. Chem. Soc. Chem. Commun., 2617-2618 (1998).
5. Hoshino, T., Kouda, M., Abe, T., and Ohashi, S., New cyclization mechanism of squalene: a ring expansion step of the five-membered C-ring intermediate in hopene biosynthesis. Biosci. Biotechnol. Biochem., 63, 2038-2041 (1999).
6. Hoshino, T., Abe, T., and Kouda, M., Unnatural natural triterpenes produced by altering isoleucine into alanine at position 261 in hopene synthase and the importance of having the appropriate bulk size at this position for directing the stereochemical destiny during the polycyclization cascade. J. Chem. Soc. Chem. Commun., 441-442 (2000).
7. Pale-Grosdemange, C., Feil, C., Rohmer, M., and Poralla, K., Occurrence of cationic intermediate and deficient control during enzymatic cyclization of squalene to hopanoids. Angew. Chem. Int. Ed., 37, 2237-2240 (1998).
8. Kannenberg, E. L. and Poralla, K., Hopanoid biosynthesis and function in bacteria. Naturwissenschaften., 86, 168-176 (1999).
9. Shibuya, M., Zhang, H., Endo, A., Shishikura, K., Kushiro, T., and Ebizuka, Y., Two branches of the lupeol synthase gene in the molecular evolution of plant oxidosqualene cyclases. Eur. J. Biochem., 266, 302-307 (1999).
10. Godzina, S., Lovato, M. A., Meyer, M. M., Foster, K. A., Wilson, W. K., Gu, W., de Hostos, E. L., and Matsuda, S. P. T., Cloning and characterization of the Dictyostelium discoideum cycloartenol synthase cDNA. Lipids, 35, 249-255 (2000).
11. Sato, T., Kanai, Y., and Hoshino, T., Overexpression of squalene-hopene cyclase by the pET vector in Escherichia coli and first identification of tryptophan and aspartic acid residues inside the QW motif as active sites. Biosci. Biotechnol. Biochem., 62, 407-411 (1998).
12. Wendt, K. U., Poralla, K., and Schulz, G. E., Structure and function of a squalene cyclase. Science, 277, 1811-1815 (1997).
13. Wendt, K. U., Lenhart, A., and Schulz, G. E., The structure of the membrane protein squalene-hopene cyclase at 2.0 Å resolution. J. Mol. Biol., 286, 175-187 (1999).
14. Sato, T. and Hoshino, T., Kinetic studies on the function of all the conserved tryptophans involved inside and outside the QW motifs of squalene-hopene cyclase: stabilizing effect of the protein structure against thermal denaturation. Biosci. Biotechnol. Biochem., 63, 1171-1180 (1999).
15. Sato, T. and Hoshino, T., Functional analysis of the DXDDTA motif in squalene-hopene cyclase by site-directed mutagenesis experiments: initiation site of the polycyclization reaction and stabilization site of the carbocation intermediate of the initially cyclized A-ring. Biosci. Biotechnol. Biochem., 63, 2189-2198 (1999).
16. Hoshino, T. and Sato, T., Functional analysis of phenylalanine 365 in hopene synthase, a conserved amino acid in the families of squalene and oxidosqualene cyclases. J. Chem. Soc. Chem. Commun., 2005-2006 (1999).
17. Hoshino, T., Kouda, M., Abe, T., and Sato, T., Functional analysis of Phe605, a conserved aromatic amino acid in squalene-hopene cyclase. J. Chem. Soc. Chem. Commun., 1485-1486 (2000).
18. Feil, C., Sussmuth, R., Jung, G., and Poralla, K., Site-directed mutagenesis of putative active-site residues in squalene-hopene cyclase. Eur. J. Biochem., 242, 51-55 (1996).
19. Merkofer, T., Pale-Grosdemange, C., Wendt, K. U., Rohmer, M., and Poralla, K., Altered product pattern of a squalene-hopene cyclase by mutagenesis of active site residues. Tetrahedron Lett., 40, 2121-2124 (1999).
20. Pale-Grosdemange, C., Merkofer, T., Rohmer, M., and Poralla, K., Production of bicyclic and tricyclic triterpenes by mutated squalene-hopene cyclase. Tetrahedron Lett., 40, 6009-6012 (1999).
21. Füll, C. and Poralla, K., Conserved Tyr residues determined function of Alicyclobacillus acidocaldarius squalene-hopene cyclase. FEMS Microbiol. Lett., 183, 221-224 (2000).
22. Shiojima, K., Arai, Y., Masuda, K., Kamada, T., and Ageta, H., Fern constituents: polypodatetraenes, novel bicyclic triterpenoids, isolated from polypodiaceous and aspidiaceous plants. Tetrahedron Lett., 24, 5733-2736 (1983).
23. Hoshino, T. and Kondo, T., The cyclization mechanism of squalene in hopene biosynthesis: the terminal methyl groups are critical to the correct folding of this substrate both for the formation of the five-membered E-ring and for the initiation of the polycyclization reaction. J. Chem. Soc. Chem. Commun., 731-732 (1999).
24. Nishino, M. and Hirota, M., CH/π interaction: implication in organic chemistry. Tetrahedron, 45, 7201-7245 (1989).
25. Dang, T. and Prestwich, G. D., Site-directed mutagenesis of squalene-hopene cyclase: altered substrate specificity and product distribution. Chem. Biol., 7, 643-649 (2000).
26. Shi, Z., Buntel, C. J., and Griffin, J. H., Isolation and characterization of the gene encoding 2,3-oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA, 91, 7370-7374 (1994).
27. Dougherty, D. A., Cation-π interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science, 271, 163-168 (1996).