Structure of l-rhamnose isomerase in complex with l-rhamnopyranose demonstrates the sugar-ring opening mechanism and the role of a substrate sub-binding site

Hiromi Yoshida, Akihide Yoshihara, Misa Teraoka, Satoshi Yamashita, Ken Izumori, Shigehiro Kamitori

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

l-Rhamnose isomerase (l-RhI) catalyzes the reversible isomerization of l-rhamnose to.l-rhamnulose. Previously determined X-ray structures of l-RhI showed a hydride-shift mechanism for the isomerization of substrates in a linear form, but the mechanism for opening of the sugar-ring is still unclear. To elucidate this mechanism, we determined X-ray structures of a mutant l-RhI in complex with l-rhamnopyranose and d-allopyranose. Results suggest that a catalytic water molecule, which acts as an acid/base catalyst in the isomerization reaction, is likely to be involved in pyranose-ring opening, and that a newly found substrate sub-binding site in the vicinity of the catalytic site may recognize different anomers of substrates.

Original languageEnglish
Pages (from-to)35-40
Number of pages6
JournalFEBS Open Bio
Volume3
DOIs
Publication statusPublished - 2013

Keywords

  • L-Rhamnose isomerase
  • Pseudomonas stutzeri
  • Rare sugar
  • Sugar-ring opening mechanism
  • X-ray structure

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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