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Literature summary for 2.4.1.248 extracted from

  • Suzuki, N.; Fujimoto, Z.; Kim, Y.M.; Momma, M.; Kishine, N.; Suzuki, R.; Suzuki, S.; Kitamura, S.; Kobayashi, M.; Kimura, A.; Funane, K.
    Structural elucidation of the cyclization mechanism of alpha-1,6-glucan by Bacillus circulans T-3040 cycloisomaltooligosaccharide glucanotransferase (2014), J. Biol. Chem., 289, 12040-12051.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the core fragment from Ser39 to Met738, devoid of its N-terminal signal peptide and C-terminal nonconserved regions. The structural model contains one catalytic (beta/alpha)8-barrel domain and three beta-domains. Domain N with an immunoglobulin-like beta-sandwich fold is attached to the N-terminus. Domain C with a Greek key beta-sandwich fold is located at the C-terminus, and a carbohydrate-binding module family 35 beta-jellyroll domain B is inserted between the 7thbeta-strand and the 7th alpha-helix of the catalytic domain A. The structures of the inactive catalytic nucleophile mutant enzyme complexed with isomaltohexaose, isomaltoheptaose, isomaltooctaose, and cycloisomaltooctaose reveal that the ligands bind in the catalytic cleft and the sugar-binding site of CBM35 Niallia circulans

Organism

Organism UniProt Comment Textmining
Niallia circulans P94286
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Niallia circulans T-3040 P94286
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information carbohydrate-binding module CBM35 functions in determining the size of the product, causing the predominant production of cycloisomaltooctaose by the enzyme. The isomaltoheptaose and cycloisomaltooctaose bind in the catalytic cleft with a circular structure around Met-310, representing the enzyme-product complex. The canonical sugar-binding site of CBM35 binds the mid-part of isomaltooligosaccharides Niallia circulans ?
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?
additional information carbohydrate-binding module CBM35 functions in determining the size of the product, causing the predominant production of cycloisomaltooctaose by the enzyme. The isomaltoheptaose and cycloisomaltooctaose bind in the catalytic cleft with a circular structure around Met-310, representing the enzyme-product complex. The canonical sugar-binding site of CBM35 binds the mid-part of isomaltooligosaccharides Niallia circulans T-3040 ?
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?
soluble starch
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Niallia circulans cyclomaltooctaose main product ?
soluble starch
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Niallia circulans T-3040 cyclomaltooctaose main product ?