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CAS1  -  cycloartenol synthase

Arabidopsis thaliana

 
 
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High impact information on CAS1

  • Oligonucleotide primers were designed corresponding to protein sequences conserved between Candida albicans ERG7 and the related Arabidopsis thaliana cycloartenol synthase [(S)-2,3-epoxysqualene mutase (cyclizing, cycloartenol forming), EC 5.4.99.8] [1].
  • Enzyme redesign: two mutations cooperate to convert cycloartenol synthase into an accurate lanosterol synthase [2].
  • This allowed use of a plasmid shuffle to select for cas1 mutants that could substitute for ERG7 activity [3].
  • A random mutagenesis/in vivo selection approach was applied to generate and identify mutations that alter the product specificity of oxidosqualene-cycloartenol synthase (CAS) from Arabidopsis thaliana [3].
  • Sequence and structural homology modeling of CAS indicate that the observed product specificity-altering mutations occur both within (Tyr410Cys, Ile481Thr, and Tyr532His) and outside of (Ala469Val and His477Tyr) the cyclase active site [3].
 

Biological context of CAS1

 

Associations of CAS1 with chemical compounds

 

Other interactions of CAS1

 

Analytical, diagnostic and therapeutic context of CAS1

References

  1. Molecular cloning, characterization, and overexpression of ERG7, the Saccharomyces cerevisiae gene encoding lanosterol synthase. Corey, E.J., Matsuda, S.P., Bartel, B. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  2. Enzyme redesign: two mutations cooperate to convert cycloartenol synthase into an accurate lanosterol synthase. Lodeiro, S., Schulz-Gasch, T., Matsuda, S.P. J. Am. Chem. Soc. (2005) [Pubmed]
  3. Conversion of a plant oxidosqualene-cycloartenol synthase to an oxidosqualene-lanosterol cyclase by random mutagenesis. Wu, T.K., Griffin, J.H. Biochemistry (2002) [Pubmed]
  4. Steric bulk at cycloartenol synthase position 481 influences cyclization and deprotonation. Matsuda, S.P., Darr, L.B., Hart, E.A., Herrera, J.B., McCann, K.E., Meyer, M.M., Pang, J., Schepmann, H.G. Org. Lett. (2000) [Pubmed]
  5. Molecular cloning and characterization of a cDNA for Glycyrrhiza glabra cycloartenol synthase. Hayashi, H., Hiraoka, N., Ikeshiro, Y., Kushiro, T., Morita, M., Shibuya, M., Ebizuka, Y. Biol. Pharm. Bull. (2000) [Pubmed]
  6. Molecular cloning of pea cDNA encoding cycloartenol synthase and its functional expression in yeast. Morita, M., Shibuya, M., Lee, M.S., Sankawa, U., Ebizuka, Y. Biol. Pharm. Bull. (1997) [Pubmed]
  7. Two branches of the lupeol synthase gene in the molecular evolution of plant oxidosqualene cyclases. Shibuya, M., Zhang, H., Endo, A., Shishikura, K., Kushiro, T., Ebizuka, Y. Eur. J. Biochem. (1999) [Pubmed]
  8. Cloning and characterization of a cDNA encoding beta-amyrin synthase involved in glycyrrhizin and soyasaponin biosyntheses in licorice. Hayashi, H., Huang, P., Kirakosyan, A., Inoue, K., Hiraoka, N., Ikeshiro, Y., Kushiro, T., Shibuya, M., Ebizuka, Y. Biol. Pharm. Bull. (2001) [Pubmed]
  9. Zymomonas mobilis squalene-hopene cyclase gene (shc): cloning, DNA sequence analysis, and expression in Escherichia coli. Reipen, I.G., Poralla, K., Sahm, H., Sprenger, G.A. Microbiology (Reading, Engl.) (1995) [Pubmed]
  10. Cloning and characterization of the Arabidopsis thaliana lupeol synthase gene. Herrera, J.B., Bartel, B., Wilson, W.K., Matsuda, S.P. Phytochemistry (1998) [Pubmed]
 
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