Conversion of β-carotene into astaxanthin: Two separate enzymes or a bifunctional hydroxylase-ketolase protein?

@article{Martn2008ConversionO,
  title={Conversion of $\beta$-carotene into astaxanthin: Two separate enzymes or a bifunctional hydroxylase-ketolase protein?},
  author={Juan Francisco Mart{\'i}n and Eduardo J. Gudi{\~n}a and Jos{\'e} Luis Barredo},
  journal={Microbial Cell Factories},
  year={2008},
  volume={7},
  pages={3 - 3}
}
Astaxanthin is a xanthophyll of great interest in animal nutrition and human health. The market prospect in the nutraceutics industries for this health-protective molecule is very promising. Astaxanthin is synthesized by several bacteria, algae and plants from β-carotene by the sequential action of two enzymes: a β-carotene, 3,3'-hydroxylase that introduces an hydroxyl group at the 3 (and 3') positions of each of the two β-ionone rings of β-carotene, and a β-carotene ketolase that introduces… Expand
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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. Expand
Novel β-carotene ketolases from non-photosynthetic bacteria for canthaxanthin synthesis
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The identification of the rest of the carotenoid synthesis genes in AN12 showed apparent homology to putative phytoene dehydrogenases, and the presence of six conserved regions may be a signature for the CrtO-type of β-carotene ketolases. Expand
Characterization of bacterial β-carotene 3,3′-hydroxylases, CrtZ, and P450 in astaxanthin biosynthetic pathway and adonirubin production by gene combination in Escherichia coli
Abstractβ-Carotene hydroxylase (CrtZ) is one of rate-limiting enzymes for astaxanthin production. A complementation analysis was conducted using Escherichia coli transformants to compare theExpand
Isolation and functional identification of a novel cDNA for astaxanthin biosynthesis from Haematococcus pluvialis, and astaxanthin synthesis in Escherichia coli
We succeeded in isolating a novel cDNA involved in astaxanthin biosynthesis from the green alga Haematococcus pluvialis, by an expression cloning method using an Escherichia coli transformant as aExpand
Expression in Escherichia coli and properties of the carotene ketolase from Haematococcus pluvialis.
TLDR
It is concluded that the carotenoids zeaxanthin and adonixanthin which accumulate in addition to astaxanthIn in this transformant are products of side reactions rather than direct precursors of astaxantin. Expand
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TLDR
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The crtS gene of Xanthophyllomyces dendrorhous encodes a novel cytochrome-P450 hydroxylase involved in the conversion of beta-carotene into astaxanthin and other xanthophylls.
TLDR
Results show that the crtS gene is involved in the conversion of beta-carotene into xanthophylls, being potentially useful to engineer carotenoid pathways. Expand
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TLDR
Surprisingly, this protein has no detectable desaturase activity with phytoene, hydroxyneurosporene, or ζ-carotene as substrates, but is rather a β-Carotene ketolase that acts asymmetrically introducing a keto group on only one of the two β-ionone rings of β- carotene to generate echinenone. Expand
Carotenoid hydroxylase from Haematococcus pluvialis: cDNA sequence, regulation and functional complementation.
  • H. Linden
  • Biology, Medicine
  • Biochimica et biophysica acta
  • 1999
TLDR
It is proposed that the carotenoid hydroxylase characterized in the present publication is involved in the biosynthesis of astaxanthin during cyst cell formation of H. pluvialis. Expand
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