Part:BBa_K4588027
Contents
4-hydroxy phenylacetate 3-monooxygenase reductase component B (S. cerevisiae), HpaB
This part encodes 4-hydroxy phenylacetate 3-monooxygenase reductase component B from Lysinibacillus capsici
Biology
The organism this gene is initially expressed in is L. capsici.
HpaB is a reduced FAD (FADH2)-utilizing monooxygenase. This enzyme component uses FADH2 and O2 to oxidize 4-hydroxyphenylacetate [1].
Usage
This enzyme is implemented in the synthesis pathway to produce rosmarinic acid in the Saccharomyces cerevisiae culture. HpaB is part of the two-step process of converting p-coumaric acid into caffeic acid, which adds a hydroxyl group onto the phenyl ring.
References
1. Xun, L., & Sandvik, E. R. (2000). Characterization of 4-hydroxyphenylacetate 3-hydroxylase (HpaB) of Escherichia coli as a reduced flavin adenine dinucleotide-utilizing monooxygenase. Applied and environmental microbiology, 66(2), 481–486. https://doi.org/10.1128/AEM.66.2.481-486.2000
2. Babaei, M., Borja Zamfir, G. M., Chen, X., Christensen, H. B., Kristensen, M., Nielsen, J., & Borodina, I. (2020). Metabolic engineering of saccharomyces cerevisiae for rosmarinic acid production. ACS Synthetic Biology, 9(8), 1978–1988. https://doi.org/10.1021/acssynbio.0c0004
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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