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Aristolochene synthase

Part of the Springer Handbook of Enzymes book series (HDBKENZYMES, volume S7)

Keywords

Reaction Type Mutant Enzyme Turnover Number Crystal Structure Determination Aspergillus Terreus 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. [1]
    Cane, D.E.; Prabhakaran, P.C.; Oliver, J.S.; McIlwaine, D.B.: Aristolochene biosynthesis. Stereochemistry of the deprotonation steps in the enzymatic cyclization of farnesyl pyrophosphate. J. Am. Chem. Soc., 112, 3209–3210 (1990)CrossRefGoogle Scholar
  2. [2]
    Cane, D.E.; Prabhakaran, P.C.; Salaski, E.J.; Harrison, P.M.H.; Noguchi, H.; Rawlings, B.J.: Aristolochene biosynthesis and enzymatic cyclization of farnesyl pyrophosphate. J. Am. Chem. Soc., 111, 8914–8916 (1989)CrossRefGoogle Scholar
  3. [3]
    Hohn, T.M.; Plattner, R.D.: Purification and characterization of the sesquiterpene cyclase aristolochene synthase from Penicillium roqueforti. Arch. Biochem. Biophys., 272, 137–143 (1989)CrossRefPubMedGoogle Scholar
  4. [4]
    Proctor, R.H.; Hohn, T.M.: Aristolochene synthase. Isolation, characterization, and bacterial expression of a sesquiterpenoid biosynthetic gene (Ari1) from Penicillium roqueforti. J. Biol. Chem., 268, 4543–4548 (1993)PubMedGoogle Scholar
  5. [5]
    Caruthers, J.M.; Kang, I.; Rynkiewicz, M.J.; Cane, D.E.; Christianson, D.W.: Crystal structure determination of aristolochene synthase from the blue cheese mold, Penicillium roqueforti. J. Biol. Chem., 275, 25533–25539 (2000)CrossRefPubMedGoogle Scholar
  6. [6]
    Calvert, M.J.; Taylor, S.E.; Allemann, R.K.: Tyrosine 92 of aristolochene synthase directs cyclisation of farnesyl pyrophosphate. Chem. Commun., 2002, 2384–2385 (2002)CrossRefGoogle Scholar
  7. [7]
    Calvert, M.J.; Ashton, P.R.; Allemann, R.K.: Germacrene A is a product of the aristolochene synthase-mediated conversion of farnesylpyrophosphate to aristolochene. J. Am. Chem. Soc., 124, 11636–11641 (2002)CrossRefPubMedGoogle Scholar
  8. [8]
    Deligeorgopoulou, A.; Allemann, R.K.: Evidence for differential folding of farnesyl pyrophosphate in the active site of aristolochene synthase: a single-point mutation converts aristolochene synthase into an (E)-β-farnesene synthase. Biochemistry, 42, 7741–7747 (2003)CrossRefPubMedGoogle Scholar
  9. [9]
    Cane, D.E.; Kang, I.: Aristolochene synthase: purification, molecular cloning, high-level expression in Escherichia coli, and characterization of the Aspergillus terreus cyclase. Arch. Biochem. Biophys., 376, 354–364 (2000)CrossRefPubMedGoogle Scholar
  10. [10]
    O’Maille, P.E.; Chappell, J.; Noel, J.P.: Biosynthetic potential of sesquiterpene synthase: alternative product of tobacco 5-epi-aristolochene synthase. Arch. Biochem. Biophys., 448, 73–82 (2006)CrossRefPubMedGoogle Scholar
  11. [11]
    Forcat, S.; Allemann, R.K.: Dual role for phenylalanine 178 during catalysis by aristolochene synthase. Chem. Commun., 2004, 2094–2095 (2004)CrossRefGoogle Scholar
  12. [12] Felicetti, B.; Cane, D.E.: Aristolochene synthase: mechanistic analysis of active site residues by site-directed mutagenesis. J. Am. Chem. Soc., 126, 7212–7221 (2004)CrossRefPubMedGoogle Scholar
  13. [13]
    Wu, S.; Schoenbeck, M.A.; Greenhagen, B.T.; Takahashi, S.; Lee, S.; Coates, R.M.; Chappell, J.: Surrogate splicing for functional analysis of sesquiterpene synthase genes. Plant Physiol., 138, 1322–1333 (2005)CrossRefPubMedGoogle Scholar

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