Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 412, Issue 2, Pages 238-244Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2011.07.073
Keywords
alpha-Neoagarobiose hydrolase; Five-bladed beta-propeller fold; Agarolytic pathway; Glycoside hydrolase family 117
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Funding
- National Research Foundation (NRF)
- Korea government (MEST) [2009-006860, 2011-0015629]
- National Research Foundation of Korea [2011-0015629] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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In agarolytic microorganisms, alpha-neoagarobiose hydrolase (NABH) is an essential enzyme to metabolize agar because it converts alpha-neoagarobiose (0-3,6-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 A. respectively. The overall fold is organized in an N-terminal helical extension and a C-terminal five-bladed beta-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. (C) 2011 Elsevier Inc. All rights reserved.
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