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  Pentalenene synthase. Analysis of active site residues by site- directed mutagenesis

Seemann, M., Zhai, G. Z., Kraker, D., Paschall, C. M., Christianson, D. W., & Cane, D. E. (2002). Pentalenene synthase. Analysis of active site residues by site- directed mutagenesis. Journal of the American Chemical Society, 124(26), 7681-7689. doi:10.1021/ja026058q.

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 Creators:
Seemann, M., Author
Zhai, G. Z., Author
Kraker, De1, Author           
Paschall, C. M., Author
Christianson, D. W., Author
Cane, D. E., Author
Affiliations:
1Department of Biochemistry, Prof. J. Gershenzon, MPI for Chemical Ecology, Max Planck Society, Jena, DE, ou_421893              

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Free keywords: Farnesyl-diphosphate synthase; high-level expression; pre- steady-state; crystal-structure; aristolochene synthase; trichodiene synthase; 5-epi-aristolochene synthase; enzymatic cyclization; sterol biosynthesis; molecular-cloning
 Abstract: Incubation of farnesyl diphosphate (1) with the W308F or W308F/H309F mutants of pentalenene synthase, an enzyme from Streptomyces UC5319, yielded pentalenene (2), accompanied by varying proportions of (+)-germacrene A (7) with relatively minor changes i

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 Dates: 2002
 Publication Status: Issued
 Pages: -
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 Rev. Type: -
 Identifiers: Other: GER034
DOI: 10.1021/ja026058q
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Title: Journal of the American Chemical Society
  Other : J. Am. Chem. Soc.
  Abbreviation : JACS
Source Genre: Journal
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Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 124 (26) Sequence Number: - Start / End Page: 7681 - 7689 Identifier: ISSN: 0002-7863
CoNE: https://pure.mpg.de/cone/journals/resource/954925376870