Crystal structure of the covalent intermediate of human cytosolic β-glucosidase

Junji Noguchi, Yasuhiro Hayashi, Yuichi Baba, Nozomu Okino, Makoto Kimura, Makoto Ito, Yoshimitsu Kakuta

Research output: Contribution to journalArticlepeer-review

20 Citations (Scopus)

Abstract

Human cytosolic β-glucosidase, also known as klotho-related protein (KLrP, GBA3), is an enzyme that hydrolyzes various β-d-glucosides, including glucosylceramide. We recently reported the crystal structure of KLrP in complex with glucose [Y. Hayashi, N. Okino, Y. Kakuta, T. Shikanai, M. Tani, H. Narimatsu, M. Ito, Klotho-related protein is a novel cytosolic neutral beta-glycosylceramidase, J. Biol. Chem. 282 (2007) 30889-30900]. Here, we report the crystal structure of a covalent intermediate of the KLrP mutant E165Q, in which glucose was covalently bound to a nucleophile, Glu373. The structure confirms the double displacement mechanism of the retaining β-glucosidase. In addition, the structure suggests that a water molecule could be involved in the stabilization of transition states through a sugar, 2-hydroxyl.

Original languageEnglish
Pages (from-to)549-552
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume374
Issue number3
DOIs
Publication statusPublished - Sep 26 2008

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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