| Bioactivity | p-Fluoro-L-phenylalanine (4-Fluoro-L-phenylalanine) is a substrate for tyrosine hydroxylase (TH) that can be used to study the regulation of that enzyme. p-Fluoro-L-phenylalanine binds to the L-leucine specific receptor of Escherichia coli (KD=0.26 μM)[1][2]. | ||||||||||||
| Name | p-Fluoro-L-phenylalanine | ||||||||||||
| CAS | 1132-68-9 | ||||||||||||
| Formula | C9H10FNO2 | ||||||||||||
| Molar Mass | 183.18 | ||||||||||||
| Appearance | Solid | ||||||||||||
| Transport | Room temperature in continental US; may vary elsewhere. | ||||||||||||
| Storage |
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| Reference | [1]. Hillas PJ, et al. A mechanism for hydroxylation by tyrosine hydroxylase based on partitioning of substituted phenylalanines. Biochemistry. 1996;35(22):6969-6975. [2]. Luck LA, et al. Fluorescence and 19F NMR evidence that phenylalanine, 3-L-fluorophenylalanine and 4-L-fluorophenylalanine bind to the L-leucine specific receptor of Escherichia coli. Protein Sci. 2000;9(12):2573-2576. |