Journal
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 69, Issue 9, Pages 1753-1759Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.69.1753
Keywords
cytochrome P450; Streptomyces; indolocarbazole; staurosporine; biosynthesis
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The staurosporine biosynthetic gene cluster in Streptomyces sp. TP-A0274 consists of 15 sta genes. In the cluster, it was predicted that staN, which shows high similarity to cytochrome P450 is involved in C-N bond formation between the nitrogen at N-12 of aglycone and the carbon at C-5' of deoxysugar. The staN disruptant produced holyrine A instead of staurosporine. The structure of holyrine A is aglycone linking to 2,3,6-trideoxy-3-aminoaldohexose between N-13 and C-1' of deoxysugar. Holyrine A was converted to staurosporine by the staD disruptant. These results indicate that StaN, cytochrome P450 is responsible for C-N bond formation. This is the first example of C-N bond formation catalyzed by cytochrome P450. In addition, holyrine A was confirmed to be an intermediate of staurosporine biosynthesis, which suggests that the N- and O-methylation at C-3' and C4 takes place after the formation of the C-N bond between C-5' and N-12 in the biosynthetic pathway.
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