NMR analysis of in vitro-synthesized proteins without purification: a high-throughput approach |
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Authors: | Guignard Laurent Ozawa Kiyoshi Pursglove Sharon E Otting Gottfried Dixon Nicholas E |
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Affiliation: | Enzyme Laboratory, National Food Research Institute, Ibaraki, Tsukuba, Japan. |
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Abstract: | The gene (agu) encoding p-nitrophenyl alpha-D-glucuronopyranoside (pNP-GUA) hydrolyzing alpha-glucuronidase of the hyperthermophilic bacterium Thermotoga maritima was cloned and expressed in Escherichia coli. The recombinant enzyme was purified and characterized. The gene previously designated as putative alpha-glucosidase was found to code for a protein that had no alpha-glucosidase activity. It showed a rare activity profile with its ability to hydrolyze pNP-GUA, an activity not known in the alpha-glucuronidases from microbial sources. This is the first report on the occurrence of an alpha-glucuronidase which belongs to the family 4 of glycosyl hydrolases. |
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