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OJBTM
Online Journal of
Bioinformatics ©
Volume 13 (1):41-49, 2012
Simulation
of riboflavin synthase in Eremothecium gossypii conversion of
6,7-dimethyl-8-ribityllumazine to riboflavin
Syarifuddin Idrus and Usman S.F. Tambunan
Departement of Chemistry, Faculty of Mathematics and
Science, University of Indonesia, Depok 16424
Indonesia.
ABSTRACT
Idrus S, Tambunan USF., Simulation of riboflavin synthase
in Eremothecium gossypii converting
6,7-dimethyl-8-ribityllumazine to riboflavin, Online J Bioinform.,
13
(1):41-49, 2012. Riboflavin
synthase catalyzes conversion of two molecules of 6,7-dimethyl-8-ribityllumazine into one of riboflavin. An In silico simulation
of riboflavin synthase of Eremothecium gossypii to convert 6,7-dimethyl-8-ribityllumazine
to riboflavin is described. Thermal
stability of the enzyme was conducted using molecular dynamic simulation at
300K, 315K, 325K, 335K, and 350K. Substrate-interacted residues were Ser152,
Thr154, Ser167, and Thr172 at the C-terminal domain and Glu22, Cys54, Thr56,
Ala70, Thr73, and His108 at the N-terminal. Only one enzyme
active site (N-terminal domain) catalyzed riboflavin formation. His108 was an active site from the
N-terminal domain, which acted at an early stage of the riboflavin catalysis
reaction.
Key words: Simulation
studies, Riboflavin synthase, Riboflavin, Eremothecium gossypii, Molecular Dynamics.