Stereospecific hydroxylation of indan by Escherichia coli containing the cloned toluene dioxygenase genes from Pseudomonas putida F1

J. M. Brand, D. L. Cruden, G. J. Zylstra, D. T. Gibson

Research output: Contribution to journalComment/debate

36 Citations (Scopus)

Abstract

Escherichia coli JM109(pDTG601), containing the todC1C2BA genes encoding toluene dioxygenase from Pseudomonas putida F1, oxidizes indan to (-)-(1R)- indanol (83% R) and trans-1,3-indandiol. Under similar conditions, P. putida F39/D oxidizes indan to (-)-(1R)-indanol (96% R), 1-indanone, and trans-1,3- indandiol. The differences in the enantiomeric composition of the 1-indanols formed by the two organisms are due to the presence of a 1-indanol dehydrogenase in P. putida F39/D that preferentially oxidizes (+)-(1S)- indanol.

Original languageEnglish (US)
Pages (from-to)3407-3409
Number of pages3
JournalApplied and environmental microbiology
Volume58
Issue number10
StatePublished - Oct 21 1992
Externally publishedYes

Fingerprint

Pseudomonas putida
toluene
hydroxylation
Hydroxylation
Escherichia coli
gene
Genes
genes
organisms
indans
indan
toluene dioxygenase
organism
1-indanol

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Food Science
  • Applied Microbiology and Biotechnology
  • Ecology

Cite this

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title = "Stereospecific hydroxylation of indan by Escherichia coli containing the cloned toluene dioxygenase genes from Pseudomonas putida F1",
abstract = "Escherichia coli JM109(pDTG601), containing the todC1C2BA genes encoding toluene dioxygenase from Pseudomonas putida F1, oxidizes indan to (-)-(1R)- indanol (83{\%} R) and trans-1,3-indandiol. Under similar conditions, P. putida F39/D oxidizes indan to (-)-(1R)-indanol (96{\%} R), 1-indanone, and trans-1,3- indandiol. The differences in the enantiomeric composition of the 1-indanols formed by the two organisms are due to the presence of a 1-indanol dehydrogenase in P. putida F39/D that preferentially oxidizes (+)-(1S)- indanol.",
author = "Brand, {J. M.} and Cruden, {D. L.} and Zylstra, {G. J.} and Gibson, {D. T.}",
year = "1992",
month = "10",
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language = "English (US)",
volume = "58",
pages = "3407--3409",
journal = "Applied and Environmental Microbiology",
issn = "0099-2240",
publisher = "American Society for Microbiology",
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}

Stereospecific hydroxylation of indan by Escherichia coli containing the cloned toluene dioxygenase genes from Pseudomonas putida F1. / Brand, J. M.; Cruden, D. L.; Zylstra, G. J.; Gibson, D. T.

In: Applied and environmental microbiology, Vol. 58, No. 10, 21.10.1992, p. 3407-3409.

Research output: Contribution to journalComment/debate

TY - JOUR

T1 - Stereospecific hydroxylation of indan by Escherichia coli containing the cloned toluene dioxygenase genes from Pseudomonas putida F1

AU - Brand, J. M.

AU - Cruden, D. L.

AU - Zylstra, G. J.

AU - Gibson, D. T.

PY - 1992/10/21

Y1 - 1992/10/21

N2 - Escherichia coli JM109(pDTG601), containing the todC1C2BA genes encoding toluene dioxygenase from Pseudomonas putida F1, oxidizes indan to (-)-(1R)- indanol (83% R) and trans-1,3-indandiol. Under similar conditions, P. putida F39/D oxidizes indan to (-)-(1R)-indanol (96% R), 1-indanone, and trans-1,3- indandiol. The differences in the enantiomeric composition of the 1-indanols formed by the two organisms are due to the presence of a 1-indanol dehydrogenase in P. putida F39/D that preferentially oxidizes (+)-(1S)- indanol.

AB - Escherichia coli JM109(pDTG601), containing the todC1C2BA genes encoding toluene dioxygenase from Pseudomonas putida F1, oxidizes indan to (-)-(1R)- indanol (83% R) and trans-1,3-indandiol. Under similar conditions, P. putida F39/D oxidizes indan to (-)-(1R)-indanol (96% R), 1-indanone, and trans-1,3- indandiol. The differences in the enantiomeric composition of the 1-indanols formed by the two organisms are due to the presence of a 1-indanol dehydrogenase in P. putida F39/D that preferentially oxidizes (+)-(1S)- indanol.

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M3 - Comment/debate

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AN - SCOPUS:0026787255

VL - 58

SP - 3407

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JO - Applied and Environmental Microbiology

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SN - 0099-2240

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