Geranyl Diphosphate:4-Hydroxybenzoate Geranyltransferase from Lithospermum erythrorhizon
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 277, Issue: 8, Page: 6240-6246
2002
- 142Citations
- 78Captures
- 1Mentions
Metric Options: CountsSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations142
- Citation Indexes142
- 142
- CrossRef107
- Captures78
- Readers78
- 63
- 15
- Mentions1
- References1
- 1
Article Description
Two cDNAs encoding geranyl diphosphate:4-hy- droxybenzoate 3-geranyltransferase were isolated from Lithospermum erythrorhizon by nested PCR using the conserved amino acid sequences among polyprenyl- transferases for ubiquinone biosynthesis. They were functionally expressed in yeast COQ2 disruptant and showed a strict substrate specificity for geranyl diphosphate as the prenyl donor, in contrast to ubiquinone biosynthetic enzymes, suggesting that they are involved in the biosynthesis of shikonin, a naphthoquinone secondary metabolite. Regulation of their expression by various culture conditions coincided with that of geranyltransferase activity and the secondary metabolites biosynthesized via this enzyme. This is the first established plant prenyltransferase that transfers the prenyl chain to an aromatic substrate.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925819824006; http://dx.doi.org/10.1074/jbc.m106387200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0037155212&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/11744717; https://linkinghub.elsevier.com/retrieve/pii/S0021925819824006; http://www.jbc.org/lookup/doi/10.1074/jbc.M106387200; https://syndication.highwire.org/content/doi/10.1074/jbc.M106387200; https://dx.doi.org/10.1074/jbc.m106387200
Elsevier BV
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