Please use this identifier to cite or link to this item: https://hdl.handle.net/10216/103592
Author(s): José P. Leite
Márcia Duarte
Ana M. Paiva
Frederico Ferreira da Silva
Pedro M. Matias
Olga C. Nunes
Luís Gales
Title: Structure-Guided Engineering of Molinate Hydrolase for the Degradation of Thiocarbamate Pesticides
Issue Date: 2015
Abstract: 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.
URI: https://hdl.handle.net/10216/103592
Related Information: info:eu-repo/grantAgreement/FCT - Fundação para a Ciência e Tecnologia/Projectos de I&DT em Todos os Domínios Científicos/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/PTDC/AAG-TEC/3909/2012|FCOMP-01-0124-FEDER-027883
Document Type: Artigo em Revista Científica Internacional
Rights: openAccess
Appears in Collections:FEUP - Artigo em Revista Científica Internacional

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