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Title Stereospecific hydroxylation of indan by Escherichia coli containing the cloned toluene dioxygenase genes from Pseudomonas putida F1
Creator/Author Brand, J.M. ; Cruden, D.L. ; Zylstra, G.J. ; Gibson, D.T. (Univ. of Iowa, Iowa City (United States))
Publication Date1992 Oct 01
OSTI IdentifierOSTI ID: 7224317
Other Number(s)ISSN0099-2240; CODEN: AEMID
Resource TypeJournal Article
Resource RelationApplied and Environmental Microbiology ; Vol/Issue: 58:10
Subject550400 -- Genetics ;560300 -- Chemicals Metabolism & Toxicology; ESCHERICHIA COLI-- GENETIC ENGINEERING;INDAN-- HYDROXYLATION;OXYGENASES-- DNA-CLONING;TOLUENE-- BIODEGRADATION; PSEUDOMONAS;RECOMBINANT DNA;STEREOCHEMISTRY
Related SubjectALKYLATED AROMATICS;AROMATICS;BACTERIA;BIOTECHNOLOGY;CHEMICAL REACTIONS;CLONING;DECOMPOSITION;DNA;DNA HYBRIDIZATION;ENZYMES;HYBRIDIZATION;HYDROCARBONS;MICROORGANISMS;NUCLEIC ACIDS;ORGANIC COMPOUNDS;OXIDOREDUCTASES;PROTEINS
Description/Abstract Escheria coli JM109(pDTG601), containing the todC1C2BA genes encoding toluene dioxygenase from Pseudomonas putida F1, oxides indan to (-)-(1R)-indanol (83{percent} R) and trans-1,3-indandiol.^Under similar conditions, P.putida F39/D oxidizes indan to (-)-(1R)-indanol (96{percent}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.
Country of PublicationUnited States
LanguageEnglish
FormatPages: 3407-3409
System Entry Date2001 May 13

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