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Química Nova

Print version ISSN 0100-4042

Abstract

SOUZA, Anivaldo Xavier de  and  SANT'ANNA, Carlos Mauricio R.. UDP-N-acetylglucosamine-enolpyruvyl transferase: determination of protonation state of active site aminoacid residues by PM6 method. Quím. Nova [online]. 2012, vol.35, n.8, pp. 1522-1586. ISSN 0100-4042.  http://dx.doi.org/10.1590/S0100-40422012000800006.

UDP-N-acetylglucosamine-enolpyruvyl transferase (MurA) catalyzes the reaction between phosphoenol pyruvate and UDP-N-acetylglucosamine. We present a theoretical approach using the semiempirical PM6 method for defining protonation state of three active site residues, K22, H125, and K160. Prior comparison with neutron diffraction data showed that PM6 accurately predicted protonation states of active site residues of b-trypsin and D-xylose isomerase. Using the same methodology with MurA crystallographic data, we conclude that when reaction intermediate is located at the active site, H125 and K22 are in protonated form and K160 in neutral form.

Keywords : UDP-N-acetylglucosamine-enolpyruvyl transferase; reaction mechanism; semiempirical method.

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