NDLI: CYP175A1 from Thermus thermophilus HB27, the first β-carotene hydroxylase of the P450 superfamily

Content Provider	Springer Nature Link
Author	Blasco, F. Kauffmann, I. Schmid, R. D.
Copyright Year	2004
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.
Starting Page	671
Ending Page	674
Page Count	4
File Format	PDF
ISSN	01757598
Journal	Applied Microbiology and Biotechnology
Volume Number	64
Issue Number	5
e-ISSN	14320614
Language	English
Publisher	Springer-Verlag
Publisher Date	2004-01-16
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Content Type	Text
Resource Type	Article
Subject	Medicine Applied Microbiology and Biotechnology Biotechnology

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CYP175A1 from Thermus thermophilus HB27, the first β-carotene hydroxylase of the P450 superfamily