CYP175A1 from Thermus thermophilus HB27, the first -carotene hydroxylase of the P450 superfamily
- 16 January 2004
- journal article
- research article
- Published by Springer Nature in Applied Microbiology and Biotechnology
- Vol. 64 (5) , 671-674
- https://doi.org/10.1007/s00253-003-1529-7
Abstract
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.Keywords
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