来自嗜热栖热菌HB27的CYP175A1，P450超家族的首个β-胡萝卜素羟化酶。
CYP175A1 from Thermus thermophilus HB27, the first beta-carotene hydroxylase of the P450 superfamily.
作者信息
Blasco F, Kauffmann I, Schmid R D
机构信息
Institute of Technical Biochemistry, University of Stuttgart, 70569, Stuttgart, Germany.
出版信息
Appl Microbiol Biotechnol. 2004 Jun;64(5):671-4. doi: 10.1007/s00253-003-1529-7. Epub 2004 Jan 16.
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 beta rings of beta-carotene to form zeaxanthin (beta,beta-carotene-3,3'-diol) in E. coli, which produces beta-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 beta-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 beta-carotene hydroxylase of the P450 superfamily.
通过在大肠杆菌中进行功能互补研究了嗜热栖热菌HB27的耐热性细胞色素P450单加氧酶CYP175A1的生物学功能。CYP175A1的基因产物在大肠杆菌中给β-胡萝卜素的两个β环添加羟基，形成玉米黄质（β,β-胡萝卜素-3,3'-二醇），该大肠杆菌由于欧文氏菌类胡萝卜素生物合成基因而产生β-胡萝卜素。此外，光谱方法显示，携带CYP175A1和雨生红球藻胡萝卜素酮醇酶cDNA的大肠杆菌能够合成羟基海胆酮。嗜热栖热菌该酶的预测氨基酸序列与其他已知的β-胡萝卜素羟化酶没有显著相似性，但与巨大芽孢杆菌的细胞色素P450单加氧酶（CYP102A1，P450 BM3）有41%的相似性。得出的结论是，CYP175 A1代表细胞色素P450超家族中一种新型的β-胡萝卜素羟化酶。
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