Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 350941
Title Cloning of the astaxanthin synthase gene from Xanthophyllomyces dendrorhous (Phaffia rhodozyma) and its assignment as a beta-carotene 3-hydroxylase/4-ketolase
Author(s) Ojima, K.; Breitenbach, J.; Visser, J.H.; Setoguchi, Y.; Tabata, K.; Hoshino, T.; Berg, J.A. van den; Sandmann, G.
Source Molecular Genetics and Genomics 275 (2006)2. - ISSN 1617-4615 - p. 148 - 158.
Department(s) Microbiological Laboratory
Publication type Refereed Article in a scientific journal
Publication year 2006
Keyword(s) escherichia-coli - functional-characterization - haematococcus-pluvialis - biosynthetic-pathway - yeast - family - host - canthaxanthin - hydroxylase - expression
Abstract A gene has been cloned from Xanthophyllomyces dendrorhous by complementation of astaxanthin formation in a ß-carotene accumulating mutant. It consists of 3,166 bp and contains 17 introns. For the ß-carotene mutant ATCC 96815, a single point mutation in the splicing sequence of intron 8 was found. The resulting improper splicing of the mRNA results in an inactive protein. The cDNA of this ß-carotene oxygenase encodes a cytochrome P450 monooxygenase belonging to the 3A subfamily. P450-specific domains were identified including a cytochrome P450 and an oxygen binding motif. Electrons are provided by a cytochrome P450 reductase. Functional characterization of the enzyme by genetic modification of X. dendrorhous demonstrated that this P450 monooxygenase is multifunctional catalyzing all steps from ß-carotene to astaxanthin formation by oxygenation of carbon 3 and 4. The reaction sequence is first 4-ketolation of ß-carotene followed by 3-hydroxylation. A hydroxylation mechanism at allylic carbon atoms has been proposed for the generation of 4-keto and 3-hydroxy groups at both ß-ionone ends
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