4-Amino-L-phenylalanine

4-Amino-L-phenylalanine (H-Phe(4-NH2)-OH) is a metabolic intermediate and an α-carbonic anhydrase (TcCA) activator with a K_a value of 0.75 μM. 4-Amino-L-phenylalanine acts through active site cavity entrance binding and a proton shuttle mechanism to enhance the catalytic rate of CO₂ hydration. 4-Amino-L-phenylalanine serves as a diamine monomer for bio-based polymer synthesis and is produced in Escherichia coli via the shikimate pathway. 4-Amino-L-phenylalanine constitutes a structural component of haptens used in immunoassay development. 4-Amino-L-phenylalanine is used for the production of Chloramphenicol (HY-B0239) and Pristinamycin I in Streptomyces venezuelae and S. pristinaespiralis, respectively. 4-Amino-L-phenylalanine is used in research related to Trypanosoma cruzi infection^[1][2][3]. In Vitro:4-Amino-L-phenylalanine production in recombinant Escherichia coli HKE6027 is increased to 4.1 g/L (40 g/L glucose; 78 h) by knocking out the ldh gene^[1].
4-Amino-L-phenylalanine is produced at 7.4 g/L with glucose as the substrate and 5.7 g/L with sorghum bagasse enzymatic hydrolysate as the substrate in the culture of recombinant Escherichia coli HKE6027, with a yield based on the enzymatic hydrolysate that is 24% lower^[1].
4-Amino-L-phenylalanine synthesis in Escherichia coli HKE6027 is inhibited by hydroxybenzaldehydes and cinnamic acid derivatives, both with an IC50 of 20 mg/L, whereas furan aldehydes exhibit only limited inhibition at a concentration of 640 mg/L^[1].
4-Amino-L-phenylalanine (15 min pre-incubation, 10 s assay) strongly activates Trypanosoma cruzi α-carbonic anhydrase (TcCA) with a K_a of 0.75 μM^[2].