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Use of inhibitors in elucidating the mechanism of an enzyme

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According to our results, the first stage of the reaction (oxidoreduction) takes place in the Pi site (energetically more favourable), with the formation of oxyanion thiohemiacetal and thioacylenzyme intermediates without acid–base assistance of His194.

Analysis of the interaction energy by residues shows that Arg249 has an important role in the ability of the enzyme to bind the G3P substrate, which interacts with NAD and other important residues, such as Cys166, Glu109, Thr167, Ser247 and Thr226, in the GAPDH active site.

The 2.2 Å crystal structure reveals that this novel homo-dimeric protein has no identifiable structural homologues.

Our biochemical data indicate that acidic patches on the convex outer surface bind RNase E.

Together with these ABPs we develop focused libraries of (competitive) inhibitors.

Together, this toolset allows us to perform a number of conceptual experiments.

Laboratório de Planejamento e Desenvolvimento de Fármacos, Instituto de Ciências Exatas e Naturais, Universidade Federal do Pará, CP 11101, Belém, Brazil E-mail: [email protected]: 55 91-32017633 Tel: 55 91-32018235 (G3P) in the presence of inorganic phosphate (Pi) and nicotinamide adenosine dinucleotide (NAD ).

The catalytic mechanism used by GAPDH has been intensively investigated.

Attachment of a reporter entity, which can be a biotin, a fluorophore, a bioorthogonal tag, a radiolabel or a combination of these, allows for the identification, visualization, identification and spatiotemporal study of the modified enzyme(s) using various techniques and in complex biological systems ranging from cell extracts, living tissue to animal models.In all domains of life, the catalysed degradation of RNA facilitates rapid adaptation to changing environmental conditions, while destruction of foreign RNA is an important mechanism to prevent host infection.We have identified a virus-encoded protein termed gp37/Dip, which directly binds and inhibits the RNA degradation machinery of its bacterial host.In the paradigm Escherichia coli RNA degradosome, this complex is built around the hydrolytic endoribonuclease RNase E, which initiates the rate-limiting step in RNA degradation (Del Campo et al., 2015; Mc Dowall et al., 1995).Subsequent degradation is carried out by the 3’-5’ phosphorolytic exoribonuclease PNPase (polynucleotide phosphorylase) assisted by the ATP-dependent helicase Rhl B (both of which are components of the degradosome assembly) and is completed by an oligo-ribonuclease which is not associated to the complex (Evguenieva-Hackenberg and Klug, 2011; Górna et al., 2012).New energy solutions are needed to meet the increasing global energy demand and solve the environmental and societal concerns related to the use of fossil energy.