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Catalytic role of conserved HQGE motif in the CE6 carbohydrate esterase family
Authors:López-Cortés Nieves  Reyes-Duarte Dolores  Beloqui Ana  Polaina Julio  Ghazi Iraj  Golyshina Olga V  Ballesteros Antonio  Golyshin Peter N  Ferrer Manuel
Institution:Institute of Catalysis, CSIC, Cantoblanco, 28049 Madrid, Spain.
Abstract:An acetylxylan esterase (R.44), belonging to the carbohydrate esterase family 6 (CE6), retrieved from bovine rumen metagenome was analyzed. Molecular modelling and site-directed mutagenesis indicated that the enzyme possesses a catalytic triad formed by Ser(14), His(231) and Glu(152). The catalytic Ser and His have been identified in highly conserved sequences GQSX and DXXH in the CE6 family, respectively, and the active-site glutamate was part of a highly conserved sequence HQGE. This motif is situated near to the so-called Block III in the CE6 family and its role in catalysis has not been identified so far.
Keywords:AA  amino acid  AXE  acetylxylan esterase  αNA  α-napthyl acetate  CE6  carbohydrate esterase family 6  FAXX  l-arabinofuranosyl-(1" target="_blank">O-[5-O-(trans-feruloyl)-α-l-arabinofuranosyl-(1  d-xylopyranosyl-(1" target="_blank">3)-O-β-d-xylopyranosyl-(1  d-xylo-pyranose]" target="_blank">4)-d-xylo-pyranose]  p-NP  p-nitrophenyl  3-D  three-dimensional
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