Journal of Proteomics & Bioinformatics
Open Access

Department of Biotechnology, College of Science, University of Tehran, Tehran, Iran

Publications

• Research   
  Flavobacterium johnsoniae Tyrosine Ammonia Lyase (Fjtal) In-Silico Structure Prediction and Molecular Docking to L-Tyrosine, P-Coumaric Acid (pHCA) and Caffeic Acid
  Author(s): Seyyed Amirrez Mousavi Majda*
  
  Responsible for the conversion of L-tyrosine to p-coumaric acid in Flavobacterium johnsoniae, FjTAL has drawn the attention of many biochemical engineers who wish to carry out a sustainable biosynthetic scheme for the production of aromatic compounds. In this study, with the aid of various computational tools, the secondary and tertiary structures of FjTAL have been predicted. The results suggest that FjTAL forms a homo-tetramer when active as a cytosolic enzyme and it is mostly consisted of alpha helices. With the aid of molecular docking, one can hypothesize that FjTAL is likely to bind to L-tyrosine, p-coumaric acid, and caffeic acid with a similar molecular mechanism and thus, p-coumaric acid and caffeic acid may exhibit a negative feedback response toward the enzyme and inhibit its activity competitively. Two distinct binding pockets have been discovered, one of which co.. View More»
  DOI: 10.35248/0974-276X.22.15.579

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