1987
DOI: 10.3109/10242428709040139
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Initial Enzymatic Steps In The Degradation Of Alpha-Pinene ByPseudomonas FluorescensNcimb 11671

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Cited by 43 publications
(21 citation statements)
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“…1). Studies of a-pinene metabolism from P. fluorescens NCIMB 11671 (Best et al 1987;Burfield et al 1989;Colocousi et al 1996) or Nocardia sp. P18.3 (Griffiths et al 1987a, b) reported that the enzyme catalyzing this reaction, a-pinene oxide lyase, lacked prosthetic groups and had no cofactor requirement.…”
Section: Introductionmentioning
confidence: 99%
“…1). Studies of a-pinene metabolism from P. fluorescens NCIMB 11671 (Best et al 1987;Burfield et al 1989;Colocousi et al 1996) or Nocardia sp. P18.3 (Griffiths et al 1987a, b) reported that the enzyme catalyzing this reaction, a-pinene oxide lyase, lacked prosthetic groups and had no cofactor requirement.…”
Section: Introductionmentioning
confidence: 99%
“…5). This pathway classically started by a-pinene oxygenation into a-pinene oxide followed by its decyclization into isonovalal by an a-pinene oxide lyase (Best, Floyd, Magalhaes, Burfield, & Rhodes, 1987). Isonovalal was then enzymatically converted into its trans isomer (novalal), a process active only with intact cells.…”
Section: Discussion About Metabolic Pathwaymentioning
confidence: 99%
“…In such cases, biocatalysis appears at first glance not to have any advantage over a chemical transformation. The same epoxide substrate, however, was efficiently degraded by Pseudomonas fluorescens and Nocardia strains to a small set of products belonging to one specific pathway (Best et al, 1987;Griffiths et al 1987;Fig. 4.2).…”
Section: Epoxidationmentioning
confidence: 99%