Structure-Guided Engineering of Molinate Hydrolase for the Degradation of Thiocarbamate Pesticides

• Tipo: Artigo em Revista Científica Internacional
• Data: 2015

Autores

José P. Leite (Autor) Outra; Márcia Duarte (Autor) Outra; Ana M. Paiva (Autor) FEUP; Frederico Ferreira da Silva (Autor) Outra; Pedro M. Matias (Autor) Outra; Olga C. Nunes (Autor) FEUP; Luís Gales (Autor) Outra

Revista

Título: PLoS ONE

Vol. 10 Nº 4

Páginas: 1-18

ISSN: 1932-6203

Editora: Public Library of Science

Indexação

ISI Web of Knowledge - 4 Citações

Scopus - 5 Citações

Projetos Associados

PTDC/AAG-TEC/3909/2012|FCOMP-01-0124-FEDER-027883 - Caracterização e aplicação de uma nova enzima (hidrolase do molinato, MolA) em processos de biorremediação

Outras Informações

ID Authenticus: P-00G-3VP

DOI: 10.1371/journal.pone.0123430

Abstract (EN): Molinate is a recalcitrant thiocarbamate used to control grass weeds in rice fields. The recently described molinate hydrolase, from Gulosibacter molinativorax ON4T, plays a key role in the only known molinate degradation pathway ending in the formation of innocuous compounds. Here we report the crystal structure of recombinant molinate hydrolase at 2.27 angstrom. The structure reveals a homotetramer with a single mononuclear metal-dependent active site per monomer. The active site architecture shows similarities with other amidohydrolases and enables us to propose a general acid-base catalysis mechanism for molinate hydrolysis. Molinate hydrolase is unable to degrade bulkier thiocarbamate pesticides such as thiobencarb which is used mostly in rice crops. Using a structural-based approach, we were able to generate a mutant (Arg187Ala) that efficiently degrades thiobencarb. The engineered enzyme is suitable for the development of a broader thiocarbamate bioremediation system.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 18