Conserved Tyr residues determine functions of Alicyclobacillus acidocaldarius squalene-hopene cyclase

FEMS Microbiology Letters

Volumn 183, Issue 2, 2000, Pages 221-224

  Füll, Christine ^a   Poralla, Karl ^a  

^a UNIVERSITY OF TÜBINGEN   (Germany)

Author keywords

Carbocation stabilization; Dammaradiene; Squalene hopene cyclase; Triterpene cyclization

Indexed keywords

HOPANOID; RECOMBINANT ENZYME; SQUALENE; SQUALENE HOPENE CYCLASE; TRITERPENOID; UNCLASSIFIED DRUG;

ALICYCLOBACILLUS ACIDOCALDARIUS; ARTICLE; BACILLUS; BACTERIUM MUTANT; CATALYSIS; CYCLIZATION; ENZYME ACTIVITY; ENZYME ASSAY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING;

BACILLUS; INTRAMOLECULAR TRANSFERASES; STRUCTURE-ACTIVITY RELATIONSHIP; TYROSINE;

EID: 0040238197     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(99)00644-8     Document Type: Article

References (11)

1. Kannenberg E.L., Poralla K. Hopanoid biosynthesis and function in bacteria. Naturwissenschaften. 86:1999;168-176.
2. Feil C., Süssmuth R., Jung G., Poralla K. Site-directed mutagenesis of putative active-site residues in squalene-hopene cyclase. Eur. J. Biochem. 242:1996;51-55.
3. Pale-Grosdemange C., Merkofer T., Rohmer M., Poralla K. Production of bicyclic and tricyclic triterpenes by mutated squalene-hopene cyclase. Tetrahedron Lett. 40:1999;6009-6012.
4. Vandeyar M.A., Weiner M.P., Hutton C.J., Batt C.A. A simple and rapid method for the selection of oligodeoxynucleotide-directed mutants. Gene. 65:1988;129-133.
5. Ochs D., Tappe C.H., Gärtner P., Kellner R., Poralla K. Properties of purified squalene-hopene cyclase from Bacillus acidocaldarius. Eur. J. Biochem. 194:1990;75-80.
6. Wendt K.U., Lenhart A., Schulz G.E. The structure of the membrane protein squalene-hopene cyclase at 2.0 Å resolution. J. Mol. Biol. 286:1999;175-187.
7. Shiojima K., Arai Y., Masuda K., Kamada T., Ageta H. Fern constituents: Polypodatetraenes, novel bicyclic triterpenoids, isolated from polypodiaceous and aspidiaceous plants. Tetrahedron Lett. 24:1983;5733-5736.
8. Pale-Grosdemange C., Feil C., Rohmer M., Poralla K. Occurrence of cationic intermediates and deficient control during the enzymatic cyclization of squalene to hopanoids. Angew. Chem. Int. Ed. 37:(16):1998;2237-2240.
9. Merkofer T., Pale-Grosdemange C., Wendt K.U., Rohmer M., Poralla K. Altered product pattern of a squalene-hopene cyclase by mutagenesis of active site residues. Tetrahedron Lett. 40:1999;2121-2124.
10. Wendt K.U., Lenhart A., Schulz G.E. The structure of the membrane protein squalene-hopene cyclase at 2.0 Å resolution. J. Mol. Biol. 286:1999;175-187.
11. Hoshino T., Sato T. Functional analysis of phenylalanine 365 in hopene synthase, a conserved amino acid in the families of squalene and oxidosqualene cyclases. Chem. Commun. 1999:1999;2005-2006.