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Title: Structure of β-1,4-mannanase from the common sea hare Aplysia kurodai at 1.05 Å resolution.
Authors: Mizutani, Kimihiko  kyouindb  KAKEN_id
Tsuchiya, Sae
Toyoda, Mayuko
Nanbu, Yuko
Tominaga, Keiko
Yuasa, Keizo
Takahashi, Nobuyuki  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0002-0196-8924 (unconfirmed)
Tsuji, Akihiko
Mikami, Bunzo  kyouindb  KAKEN_id
Author's alias: 三上, 文三
Keywords: mannanases
hemicellulose
secretory proteins
Issue Date: Oct-2012
Publisher: International Union of Crystallography
Journal title: Acta crystallographica. Section F, Structural biology and crystallization communications
Volume: 68
Issue: Part 10
Start page: 1164
End page: 1168
Abstract: 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.
Rights: © 2012 International Union of Crystallography
URI: http://hdl.handle.net/2433/161049
DOI(Published Version): 10.1107/S1744309112037074
PubMed ID: 23027740
Appears in Collections:Journal Articles

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