Stereospecific oxidation of (R)- and (S)-1-indanol by naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816-4
Article Abstract:
Napthalene dioxygenase (NDO) is a multicomponent bacterial enzyme produced by the nahAaAbAcAd gene cluster that oxidizes (R)- and (S)-1-indanol to trans-1,3-indandiol. The Pseudomonas sp. NDO expressed by the recombinant Escherichia coli produces cis-1,3-indandiol and trans-(1S,3S)-indan-1,3-diol after catalyzing the monohydroxylation, desaturation, dihydroxylation and alcohol oxidation of (R)- and (S)-1-indanol. Furthermore, the formation of 1,3-diol and 1,2,3-triol stereoisomers by NDO stems from the preexisting stereochemistry of the substrate.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1997
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Toluene and ethylbenzene oxidation by purified naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816-4
Article Abstract:
Purified naphthalene dioxygenase (NDO) from Pseudomonas sp. strain NCIB 9816-4 oxidizes ethylbenzene to 2-hydroxyacetophenone, and toluene to benzyl alcohol and benzaldehyde. The toluene oxidation involves benzylic monooxygenation and dioxygen-dependent alcohol oxidation to form benzyl alcohol and benzaldehyde respectively. The oxidation of ethylbenzene occurs sequentially through (S)-1-phenethyl alcohol and acetophenone. NDO also oxidizes ethylbenzene to (R)-1-phenyl-1,2-ethanediol though desaturation and dihydroxylation.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
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