The quinohaemoprotein lupanine hydroxylase from Pseudomonas putida

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dc.contributor.author Hopper, David J.
dc.contributor.author Kaderbhai, Mustak A.
dc.date.accessioned 2010-03-04T15:52:13Z
dc.date.available 2010-03-04T15:52:13Z
dc.date.issued 2003-02-08
dc.identifier.citation Hopper , D J & Kaderbhai , M A 2003 , ' The quinohaemoprotein lupanine hydroxylase from Pseudomonas putida ' pp. 1-2 . en
dc.identifier.other PURE: 137236
dc.identifier.other dspace: 2160/4172
dc.identifier.uri http://hdl.handle.net/2160/4172
dc.description Hopper, D. J., Kaderbhai, M. A. (2003). The quinohaemoprotein lupanine hydroxylase from Pseudomonas putida. Biochimica et Biophysica Acta-Proteins and Proteomics, 1647, (1-2), 110-115. 3rd International Symposium on Vitamin B6, PQQ, Carbonyl Catalysts and Quinoproteins, Southampton, 14th?19th April 2003. en
dc.description.abstract Lupanine hydroxylase catalyses the first reaction in the catabolism of the alkaloid lupanine by Pseudomonas putida. It dehydrogenates the substrate, which can then be hydrated. It is a monomeric protein of Mr 72,000 and contains a covalently bound haem and a molecule of PQQ. The gene for this enzyme has been cloned and sequenced and the derived protein sequence has a 26 amino acid signal sequence at the N-terminal for translocation of the protein to the periplasm. Many of the features seen in the sequence of lupanine hydroxylase are common with other quinoproteins including the W-motifs that are characteristic of the eight-bladed propeller structure of methanol dehydrogenase. However, the unusual disulfide bridge between adjacent cysteines that is present in some PQQ-containing enzymes is absent in lupanine hydroxylase. The C-terminal domain contains characteristics of a cytochrome c and overall the sequence shows similarities with that of the quinohaemoprotein, alcohol dehydrogenase from Comamonas testosteroni. The gene coding for lupanine hydroxylase has been successfully expressed in Escherichia coli and a procedure has been developed to renature and reactivate the enzyme, which was found to be associated with the inclusion bodies. Reactivation required addition of PQQ and was dependent on calcium ions. en
dc.format.extent 2 en
dc.language.iso eng
dc.relation.ispartof en
dc.title The quinohaemoprotein lupanine hydroxylase from Pseudomonas putida en
dc.type Text en
dc.type.publicationtype Conference paper en
dc.identifier.doi http://dx.doi.org/10.1016/S1570-9639(03)00070-0
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Non peer reviewed en


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