We are analyzing https://link.springer.com/article/10.1007/s00438-005-0072-x.

Title:
Cloning of the astaxanthin synthase gene from Xanthophyllomyces dendrorhous (Phaffia rhodozyma) and its assignment as a β-carotene 3-hydroxylase/4-ketolase | Molecular Genetics and Genomics
Description:
A gene has been cloned from Xanthophyllomyces dendrorhous by complementation of astaxanthin formation in a β-carotene accumulating mutant. It consists of 3,166 bp and contains 17 introns. For the β-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 β-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 β-carotene to astaxanthin formation by oxygenation of carbon 3 and 4. The reaction sequence is first 4-ketolation of β-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 β-ionone ends.
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Keywords {🔍}

google, scholar, article, cas, pubmed, astaxanthin, gene, dendrorhous, xanthophyllomyces, sandmann, βcarotene, rhodozyma, cytochrome, carotenoid, biosynthesis, phaffia, cloning, visser, van, yeast, misawa, molecular, functional, characterization, access, biotechnol, privacy, cookies, content, research, carotenoids, biosynthetic, verdoes, information, publish, search, genomics, synthase, kazuyuki, ojima, breitenbach, hoshino, sequence, monooxygenase, engineering, pathway, johnson, isolation, appl, microbiol,

Topics {✒️}

month download article/chapter kazuyuki tabata & tatsuo hoshino epoxide hydroxylase-encoding gene short amino-terminal segment β-carotene 3-hydroxylase/4-ketolase red-pigmented fermenting yeast β-carotene accumulating mutant β-carotene oxygenase encodes β-carotene producing mutants ß-carotene hydroxylase gene host-plant allelochemical resistance high-light-dependent upregulation cytochrome p450 reductase carotenoid ketolase genes article molecular genetics full article pdf β-carotene hydroxylase privacy choices/manage cookies cyanobacterium synechocystis sp carotenoid biosynthetic pathway van ooyen aj van ooyen ajj hydrocarbon β-carotene carotenoid biosynthetic gene yeast xanthophyllomyces dendrorhous astaxanthin biosynthetic pathway carotenoid hyperproducing mutants metabolic engineering p450-specific domains cytochrome p450 family tatsuo hoshino astaxanthin synthase gene β-ionone ends xanthophyllomyces dendrorhous leading antibiotic resistance cassettes gene products espressed verdoes jc functional recombinant p450s related subjects thermus thermophilus hb27 grant qlk1-ct-2001-00780 dyadic nederland bv gerhard sandmann yeast pfaffia rhodozyma conditions privacy policy p450 monooxygenase hans visser single point mutation resulting improper splicing oxygen binding motif

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            Cytochrome P450
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      headline:Cloning of the astaxanthin synthase gene from Xanthophyllomyces dendrorhous (Phaffia rhodozyma) and its assignment as a β-carotene 3-hydroxylase/4-ketolase
      description:A gene has been cloned from Xanthophyllomyces dendrorhous by complementation of astaxanthin formation in a β-carotene accumulating mutant. It consists of 3,166 bp and contains 17 introns. For the β-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 β-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 β-carotene to astaxanthin formation by oxygenation of carbon 3 and 4. The reaction sequence is first 4-ketolation of β-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 β-ionone ends.
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         Cytochrome P450
         Genetic complementation
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         Microbial Genetics and Genomics
         Animal Genetics and Genomics
         Biochemistry
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