Crystal structure of Ruminococcus albus cellobiose 2-epimerase: Structural insights into epimerization of unmodified sugar

Takaaki Fujiwara, Wataru Saburi, Sota Inoue, Haruhide Mori, Hirokazu Matsui, Isao Tanaka, Min Yao

研究成果: Article査読

27 被引用数 (Scopus)

抄録

Enzymatic epimerization is an important modification for carbohydrates to acquire diverse functions attributable to their stereoisomers. Cellobiose 2-epimerase (CE) catalyzes interconversion between d-glucose and d-mannose residues at the reducing end of β-1,4-linked oligosaccharides. Here, we solved the structure of Ruminococcus albus CE (RaCE). The structure of RaCE showed strong similarity to those of N-acetyl-d-glucosamine 2-epimerase and aldose-ketose isomerase YihS with a high degree of conservation of residues around the catalytic center, although sequence identity between them is low. Based on structural comparison, we found that His184 is required for RaCE activity as the third histidine added to two essential histidines in other sugar epimerases/isomerases. This finding was confirmed by mutagenesis, suggesting a new catalytic mechanism for CE involving three histidines. Structured summary of protein interactions: RaCE and X-ray crystallography (View interaction).

本文言語English
ページ(範囲)840-846
ページ数7
ジャーナルFEBS Letters
587
7
DOI
出版ステータスPublished - 2013 4 2
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

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