A cytochrome c from a lupanine-transforming Pseudomonas putida strain is expressed in Escherichia coli during aerobic cultivation and efficiently exported and assembled in the periplasm

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dc.contributor.author Kaderbhai, Mustak A.
dc.contributor.author Abbas, Syed K.
dc.contributor.author Kaderbhai, Naheed N.
dc.contributor.author Hopper, David J.
dc.contributor.author Akhtar, Kalim M.
dc.date.accessioned 2009-11-10T13:04:55Z
dc.date.available 2009-11-10T13:04:55Z
dc.date.issued 2003-08
dc.identifier.citation Kaderbhai , M A , Abbas , S K , Kaderbhai , N N , Hopper , D J & Akhtar , K M 2003 , ' A cytochrome c from a lupanine-transforming Pseudomonas putida strain is expressed in Escherichia coli during aerobic cultivation and efficiently exported and assembled in the periplasm ' Applied and Environmental Microbiology , vol 69 , no. 8 , pp. 4727-4731 . en
dc.identifier.other PURE: 138443
dc.identifier.other dspace: 2160/3482
dc.identifier.uri http://hdl.handle.net/2160/3482
dc.description Kaderbhai, M. A., Hopper, D. J., Akhtar, K. M., Abbas, S. K., Kaderbhai, N. N. (2003). A cytochrome c from a lupanine-transforming Pseudomonas putida strain is expressed in Escherichia coli during aerobic cultivation and efficiently exported and assembled in the periplasm. Applied and Environmental Microbiology. 69, (8), 4727-4731. RAE2008 en
dc.description.abstract We have cloned, sequenced, and heterologously expressed a periplasmic cytochrome c from a lupanine-utilizing Pseudomonas putida strain. Aerobic batch cultivation of Escherichia coli TB1 harboring the cytochrome c gene placed downstream of the lac promoter in pUC9 vector resulted in significant production of the holo-cytochrome c in the periplasm (4 mg of hemoprotein/liter of culture). The recombinant cytochrome c was purified to homogeneity and was found to be functional in accepting electrons from lupanine hydroxylase while catalyzing hydroxylation of lupanine. Comparison of the N-terminal amino acid sequence of the isolated cytochrome c with that deduced from the DNA sequence indicated that the signal sequence was processed at the bond position predicted by the SigPep program. The molecular size of the cytochrome c determined by electrospray mass spectrometry (9,595) was in precise agreement with that predicted from the nucleotide sequence. en
dc.format.extent 5 en
dc.language.iso eng
dc.relation.ispartof Applied and Environmental Microbiology en
dc.title A cytochrome c from a lupanine-transforming Pseudomonas putida strain is expressed in Escherichia coli during aerobic cultivation and efficiently exported and assembled in the periplasm en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.identifier.doi http://dx.doi.org/10.1128/AEM.69.8.4727-4731.2003
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


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