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Publication Abstract from PubMed

beta-1,4-Mannanase (EC 3.2.1.78) catalyzes the hydrolysis of beta-1,4-glycosidic bonds within mannan, a major constituent group of the hemicelluloses. Bivalves and gastropods possess beta-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 beta-1,4-mannanase prepared from the common sea hare Aplysia kurodai, was determined at 1.05 A resolution. This is the first report of the three-dimensional structure of a gastropod beta-1,4-mannanase. The structure was compared with bivalve beta-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.

Structure of beta-1,4-mannanase from the common sea hare Aplysia kurodai at 1.05 A resolution.,Mizutani K, Tsuchiya S, Toyoda M, Nanbu Y, Tominaga K, Yuasa K, Takahashi N, Tsuji A, Mikami B Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Oct 1;68(Pt 10):1164-8., doi: 10.1107/S1744309112037074. Epub 2012 Sep 25. PMID:23027740^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.