TAILIEUCHUNG - Báo cáo khoa học: Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger

Feruloyl esterases hydrolyse phenolic groups involved in the cross-linking of arabinoxylan to other polymeric structures. This is important for open-ing the cell wall structure making material more accessible to glycoside hydrolases. Here we describe the crystal structure of inactive S133A mutant of type-A feruloyl esterase fromAspergillus niger(AnFaeA) in complex with a feruloylated trisaccharide substrate. | iFEBS Journal Probing the determinants of substrate specificity of a feruloyl esterase AnFaeA from Aspergillus niger Craig B. Faulds1 Rafael Molina2 Ramon Gonzalez3 Fiona Husband1 Nathalie Juge1 4 Julia Sanz-Aparicio2 and Juan A. Hermoso2 1 Institute of Food Research Colney Norwich UK 2 Grupo de Cristalografia Macromolecular y Biologia Estructural Instituto de Quimica Fisica Rocasolano CSIC Madrid Spain 3 Departamento de Microbiologia Instituto de Fermentaciones Industriales CSIC Madrid Spain 4 Institut Mediterraneen de Recherche en Nutrition Universite PaulCezanne Marseille France Keywords active site specificity Aspergillus niger ferulic acid feruloylesterase plant cell wall Correspondence C. B. Faulds Institute of Food Research Norwich Research Park Colney Norwich NR4 7UA UK Fax 44 160 350 7723 Tel 44 160 325 5152 E-mail Received 10 March 2005 revised 27 May 2005 accepted 7 July 2005 doi Feruloyl esterases hydrolyse phenolic groups involved in the cross-linking of arabinoxylan to other polymeric structures. This is important for opening the cell wall structure making material more accessible to glycoside hydrolases. Here we describe the crystal structure of inactive S133A mutant of type-A feruloyl esterase from Aspergillus niger AnFaeA in complex with a feruloylated trisaccharide substrate. Only the ferulic acid moiety of the substrate is visible in the electron density map showing interactions through its OH and OCH3 groups with the hydroxyl groups of Tyr80. The importance of aromatic and polar residues in the activity of AnFaeA was also evaluated using site-directed mutagenesis. Four mutant proteins were heterologously expressed in Pichia pastoris and their kinetic properties determined against methyl esters of ferulic sinapic caffeic and p-coumaric acid. The kcat of Y80S Y80V W260S and W260V was drastically reduced compared to that of the wild-type enzyme. However the replacement of Tyr80 and Trp260 .

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