Structure of human alpha-enolase (hENO1), a multifunctional glycolytic enzyme.
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Kang HJ, Jung SK, Kim SJ, Chung SJ
Structure of human alpha-enolase (hENO1), a multifunctional glycolytic enzyme.
Acta Crystallogr D Biol Crystallogr. 2008 Jun;64(Pt 6):651-7. doi: 10.1107/S0907444908008561. Epub 2008 May 14.
- PubMed ID
- 18560153 [ View in PubMed]
- 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.