Structure of β-1,4-mannanase from the common sea hare Aplysia kurodai at 1.05 Å resolution.

نویسندگان

  • Kimihiko Mizutani
  • Sae Tsuchiya
  • Mayuko Toyoda
  • Yuko Nanbu
  • Keiko Tominaga
  • Keizo Yuasa
  • Nobuyuki Takahashi
  • Akihiko Tsuji
  • Bunzo Mikami
چکیده

β-1,4-Mannanase (EC 3.2.1.78) catalyzes the hydrolysis of β-1,4-glycosidic bonds within mannan, a major constituent group of the hemicelluloses. Bivalves and gastropods possess β-1,4-mannanase and may degrade mannan in seaweed and/or phytoplankton to obtain carbon and energy using the secreted enzymes in their digestive systems. In the present study, the crystal structure of AkMan, a gastropod β-1,4-mannanase prepared from the common sea hare Aplysia kurodai, was determined at 1.05 Å resolution. This is the first report of the three-dimensional structure of a gastropod β-1,4-mannanase. The structure was compared with bivalve β-1,4-mannanase and the roles of residues in the catalytic cleft were investigated. No obvious binding residue was found in subsite +1 and the substrate-binding site was exposed to the molecular surface, which may account for the enzymatic properties of mannanases that can digest complex substrates such as glucomannan and branched mannan.

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منابع مشابه

cDNA cloning and bacterial expression of an endo-β-1,4-mannanase, AkMan, from Aplysia kurodai.

Previously we isolated an endo-β-1,4-mannanase (EC 3.2.1.78), AkMan, from the digestive fluid of a common sea hare Aplysia kurodai and demonstrated that this enzyme had a broad pH optimum spanning 4.0 to 7.5 and an appreciably high heat stability in this pH range (Zahura et al., Comp. Biochem. Physiol., B157, 137-148 (2010)). In the present study, we cloned the cDNA encoding AkMan and construct...

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عنوان ژورنال:
  • Acta crystallographica. Section F, Structural biology and crystallization communications

دوره 68 Pt 10  شماره 

صفحات  -

تاریخ انتشار 2012