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UDP-N-acetilglicosamina enolpiruvil transferase: determinação dos estados de protonação de resíduos de aminoácidos do sítio ativo pelo método PM6

2012; Brazilian Chemical Society; Volume: 35; Issue: 8 Linguagem: Inglês

10.1590/s0100-40422012000800006

ISSN

1678-7064

Autores

Anivaldo Xavier de Souza, Carlos Maurício R. Sant’Anna,

Tópico(s)

Enzyme Catalysis and Immobilization

Resumo

ACTIVE SITE AMINOACID RESIDUES BY PM6 METHOD.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.

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