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

• Type: Article in International Scientific Journal
• Date: 2015

Authors

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

Journal

Title: PLoS ONE

Vol. 10 No. 4

Pages: 1-18

ISSN: 1932-6203

Publisher: Public Library of Science

Indexing

ISI Web of Knowledge - 4 Citations

Scopus - 5 Citations

Associated Projects

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

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 18