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


ABSTRACT: ?-1,4-Mannanase (EC 3.2.1.78) catalyzes the hydrolysis of ?-1,4-glycosidic bonds within mannan, a major constituent group of the hemicelluloses. Bivalves and gastropods possess ?-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 ?-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 ?-1,4-mannanase. The structure was compared with bivalve ?-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.

SUBMITTER: Mizutani K 

PROVIDER: S-EPMC3497972 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature

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

Mizutani Kimihiko K   Tsuchiya Sae S   Toyoda Mayuko M   Nanbu Yuko Y   Tominaga Keiko K   Yuasa Keizo K   Takahashi Nobuyuki N   Tsuji Akihiko A   Mikami Bunzo B  

Acta crystallographica. Section F, Structural biology and crystallization communications 20120925 Pt 10


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.  ...[more]

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