Study of Thermal Stability of Riboflavin Synthase of Eremothecium gossypii Through Molecular Dynamics Approach

Authors

  • Syarifuddin Idrus University of Indonesia
  • Usman S. F. Tambunan University of Indonesia

Keywords:

Thermal stability, riboflavin, riboflavin synthase, 6,7-dimethyl-8-ribityllumazine, molecular dynamics, Eremothecium gossypii

Abstract

Eremothecium  gossypii  has  the  enzymes  that  able  to  produce  riboflavin  naturally.  The enzyme  that  responsible  for  the  final  production  of  riboflavin  is  riboflavin  synthase. Riboflavin synthase catalyzes conversion of two molecules of 6,7-dimethyl-8-ribityllumazine into each one molecule riboflavin and 4-ribitylamino-5-aminouracil. In this study, we determined the interaction of riboflavin synthase isolated from Eremothecium gossypii with 6,7-dimethyl-8-ribityllumazine. We performed a computational approach to see the active sites of riboflavin synthase that play a role in the production of riboflavin. We designed riboflavin synthase isolated from Eremothecium gossypii as a model in PDB format. As a template, the structure of riboflavin synthase isolated from Schizosaccharomyces pombe with 1KZL PDB code was used. The thermal stability of enzyme had been conducted on the molecular dynamics simulation approach at 300K, 310K, 315K, 325K, 335K, and 350K. The results showed that amino acid residues which interact include Thr154, Ile169, Thr172, Val6, and Gly102 at the C-terminal domain and Thr56, Gly68, Ala70, Val109, and His108 at the N-terminal domain. Residue Thr154 was from the C-terminal domain and His108 was from the N-terminal domain, represents two-subunit of the enzyme that acts as an early stage at riboflavin catalysis reaction. These results shown that only one of active sites of the enzyme (N-terminal  domain) catalyze riboflavin formation. Molecular  dynamics  simulation showed the calculation of RMSD values at 300 K and 315 were fluctuated in the range of 22-26 ? from the initial state. At 320 K and 335 K, fluctuation occurred in the range of 29-34 ?. At 350 K, fluctuation occurred in 38-45 ? and the domains structure had separated.

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Published

2011-10-31

How to Cite

Idrus, S. ., & Tambunan, U. S. F. . (2011). Study of Thermal Stability of Riboflavin Synthase of Eremothecium gossypii Through Molecular Dynamics Approach. Proceeding ICBB (The International Conference on Bioscience and Biotechnology), 1(1), A101-A106. Retrieved from https://sunankalijaga.org/prosiding/index.php/icbb/article/view/159

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