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Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
Published on: June 20, 2019
Structure of human alpha-enolase (hENO1), a multifunctional glycolytic enzyme
Hyo Jin Kang1, Suk-Kyeong Jung, Seung Jun Kim
1BioNanotechnology Research Center, Korea Research Institute of Bioscience and Biotechnology and Division of Nanobiotechnology, Korea University of Science and Technology (UST), Yuseong, Daejeon 305-333, Republic of Korea.
Abstract:
Aside from its enzymatic function in the glycolytic pathway, alpha-enolase (ENO1) has been implicated in numerous diseases, including metastatic cancer, autoimmune disorders, ischaemia and bacterial infection. The disease-related roles of ENO1 are mostly attributed to its immunogenic capacity, DNA-binding ability and plasmin(ogen) receptor function, which are significantly affected by its three-dimensional structure and surface properties, rather than its enzymatic activity. Here, the crystal structure of human ENO1 (hENO1) is presented at 2.2 A resolution. Despite its high sequence similarity to other enolases, the hENO1 structure exhibits distinct surface properties, explaining its various activities, including plasmin(ogen) and DNA binding.
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