Please use this identifier to cite or link to this item: https://doi.org/10.1006/bbrc.1994.2546
DC FieldValue
dc.titleSubstitution of the ISP α subunit of biphenyl dioxygenase from Pseudomonas results in a modification of the enzyme activity
dc.contributor.authorTan, H.-M.
dc.contributor.authorCheong, C.-M.
dc.date.accessioned2014-11-10T08:47:23Z
dc.date.available2014-11-10T08:47:23Z
dc.date.issued1994
dc.identifier.citationTan, H.-M., Cheong, C.-M. (1994). Substitution of the ISP α subunit of biphenyl dioxygenase from Pseudomonas results in a modification of the enzyme activity. Biochemical and Biophysical Research Communications 204 (2) : 912-917. ScholarBank@NUS Repository. https://doi.org/10.1006/bbrc.1994.2546
dc.identifier.issn0006291X
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/107653
dc.description.abstractWe have constructed a hybrid multicomponent dioxygenase gene cluster in which the bphA1 gene, coding for ISP α subunit of biphenyl dioxygenase from Pseudomonas pseudoalcaligenes KF707, has been replaced by the bedC1 gene encoding the corresponding subunit of benzene dioxygenase from P. putida ML2. Escherichia coli cells containing the chimeric dioxygenase acquired the novel capability of producing indigo from indole. Furthermore, when compared to biphenyl dioxygenase, the hybrid dioxygenase enzyme was half as active towards benzene but exhibited only 4% activity when biphenyl was the substrate. The results implicate the ISP α subunit to be involved in substrate specificity and activity of the dioxygenase enzyme.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1006/bbrc.1994.2546
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentMICROBIOLOGY
dc.description.doi10.1006/bbrc.1994.2546
dc.description.sourcetitleBiochemical and Biophysical Research Communications
dc.description.volume204
dc.description.issue2
dc.description.page912-917
dc.description.codenBBRCA
dc.identifier.isiutA1994PN63400068
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