We are analyzing https://link.springer.com/article/10.1007/s00253-003-1529-7.

Title:
CYP175A1 from Thermus thermophilus HB27, the first β-carotene hydroxylase of the P450 superfamily | Applied Microbiology and Biotechnology
Description:
The biological function of thermostable P450 monooxygenase CYP175A1 from Thermus thermophilus HB27 was studied by functional complementation in Escherichia coli. The gene product of CYP175A1 added hydroxyl groups to both β rings of β-carotene to form zeaxanthin (β,β-carotene-3,3′-diol) in E. coli, which produces β-carotene due to the Erwinia uredovora carotenoid biosynthesis genes. In addition, spectroscopic methods revealed that E. coli carrying CYP175A1 and the cDNA of the Haematococcus pluvialis carotene ketolase was able to synthesise hydroxyechinenone. The predicted amino acid sequence of the enzyme from T. thermophilus does not show substantial similarity with other known β-carotene hydroxylases, but 41% with the cytochrome P450 monooxygenase from Bacillus megaterium (CYP102A1, P450 BM3). It is concluded that CYP175 A1 represents a new type of β-carotene hydroxylase of the P450 superfamily.
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Keywords {🔍}

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Topics {✒️}

month download article/chapter beta-carotene hydroxylase gene article applied microbiology gene products expressed related subjects produces β-carotene due privacy choices/manage cookies vitro carotenoid biosynthesis full article pdf cyanobacterium synechocystis sp cytochrome p450 hydroxylase cytochrome p450 monooxygenase thermostable cytochrome p450 carotenoid-glycoside-esters coli carrying cyp175a1 β-carotene hydroxylase european economic area scope submit manuscript spectroscopic methods revealed show substantial similarity cyp175 a1 represents 3β-ester derivatives conditions privacy policy β-carotene hydroxylases carotenoid hydroxylase thermus thermophilus hb27 accepting optional cookies nadph-flavodoxin reductase author information authors main content log form zeaxanthin journal finder publish check access astaxanthin accumulation financial support instant access article log escherichia coli article cite p450 superfamily protein products carotene ketolase article blasco gene product crtb gene gene level gene combination privacy policy personal data β-carotene

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         description:The biological function of thermostable P450 monooxygenase CYP175A1 from Thermus thermophilus HB27 was studied by functional complementation in Escherichia coli. The gene product of CYP175A1 added hydroxyl groups to both β rings of β-carotene to form zeaxanthin (β,β-carotene-3,3′-diol) in E. coli, which produces β-carotene due to the Erwinia uredovora carotenoid biosynthesis genes. In addition, spectroscopic methods revealed that E. coli carrying CYP175A1 and the cDNA of the Haematococcus pluvialis carotene ketolase was able to synthesise hydroxyechinenone. The predicted amino acid sequence of the enzyme from T. thermophilus does not show substantial similarity with other known β-carotene hydroxylases, but 41% with the cytochrome P450 monooxygenase from Bacillus megaterium (CYP102A1, P450 BM3). It is concluded that CYP175 A1 represents a new type of β-carotene hydroxylase of the P450 superfamily.
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      headline:CYP175A1 from Thermus thermophilus HB27, the first β-carotene hydroxylase of the P450 superfamily
      description:The biological function of thermostable P450 monooxygenase CYP175A1 from Thermus thermophilus HB27 was studied by functional complementation in Escherichia coli. The gene product of CYP175A1 added hydroxyl groups to both β rings of β-carotene to form zeaxanthin (β,β-carotene-3,3′-diol) in E. coli, which produces β-carotene due to the Erwinia uredovora carotenoid biosynthesis genes. In addition, spectroscopic methods revealed that E. coli carrying CYP175A1 and the cDNA of the Haematococcus pluvialis carotene ketolase was able to synthesise hydroxyechinenone. The predicted amino acid sequence of the enzyme from T. thermophilus does not show substantial similarity with other known β-carotene hydroxylases, but 41% with the cytochrome P450 monooxygenase from Bacillus megaterium (CYP102A1, P450 BM3). It is concluded that CYP175 A1 represents a new type of β-carotene hydroxylase of the P450 superfamily.
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         Synechocystis
         CYP175A1 Gene
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