Crystal structure of a key enzyme in the agarolytic pathway, α-neoagarobiose hydrolase from Saccharophagus degradans 2-40

Sung Chul Ha, Saeyoung Lee, Jonas Lee, Hee Taek Kim, Hyeok Jin Ko, Kyoung Heon Kim, In-Geol Choi

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53 Citations (Scopus)


In agarolytic microorganisms, α-neoagarobiose hydrolase (NABH) is an essential enzyme to metabolize agar because it converts α-neoagarobiose (O-3,6-anhydro-alpha-l-galactopyranosyl-(1,3)-d-galactose) into fermentable monosaccharides (d-galactose and 3,6-anhydro-l-galactose) in the agarolytic pathway. NABH can be divided into two biological classes by its cellular location. Here, we describe a structure and function of cytosolic NABH from Saccharophagus degradans 2-40 in a native protein and d-galactose complex determined at 2.0 and 1.55. Å, respectively. The overall fold is organized in an N-terminal helical extension and a C-terminal five-bladed β-propeller catalytic domain. The structure of the enzyme-ligand (d-galactose) complex predicts a +1 subsite in the substrate binding pocket. The structural features may provide insights for the evolution and classification of NABH in agarolytic pathways.

Original languageEnglish
Pages (from-to)238-244
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 2011 Aug 26



  • α-Neoagarobiose hydrolase
  • Agarolytic pathway
  • Five-bladed β-propeller fold
  • Glycoside hydrolase family 117

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

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