Synthesis of Aminoacyl Proline


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Dr. Kuniki Kino working as a professor in the Department of Applied Chemistry at Waseda University. His research article explains about the Aminoacyl proline synthesis coupled with ATP regeneration using pyruvate phosphate dikinase. Aminoacyl prolines (Xaa-Pro) are valuable materials because they exhibit antihypertensive and hypoglycemic activities. We had previously developed a novel method of amide bond formation using the adenylation domain of nonribosomal peptide synthetase that enabled us to synthesize Xaa-Pro enzymatically. However, this method has two significant issues - the supply of ATP for amino acid activation and inhibition of the adenylation reaction caused by pyrophosphate released from the reaction. To address both of these issues, we focused on pyruvate phosphate dikinase (PPDK), which converts AMP, pyrophosphate, and phosphoenolpyruvate to ATP, phosphate, and pyruvate. We constructed an ATP regeneration system using AaPPDK, a PPDK from Acetobacter aceti NBRC 14818T, and applied this system to L-Trp-L-Pro synthesis by the adenylation domain of tyrocidine synthetase A (TycA-A). Using this system, L-Trp-L-Pro production from 1 mM ATP increased to 1.83 mM (2.7-fold), and 0.94 mM L-Trp-L-Pro was synthesized from 1 mM AMP.

In conclusion, authors have demonstrated two significant effects of AaPPDK on L-Trp-L-Pro synthesis, that is, ATP regeneration from AMP and improving reaction rate by removal of PPi. We previously reported three A domains displaying different substrate specificities and that seven types of Xaa-Pro could be synthesized, including L-Trp-L-Pro. In addition, A domains activating each proteogenic amino acid might exist in nature. Therefore, we speculate that various Xaa-Pro can be synthesized efficiently by introducing the ATP regeneration system from AMP by employing AaPPDK.

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