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Literature summary for 2.4.1.230 extracted from

  • Yamamoto, T.; Yamashita, H.; Mukai, K.; Watanabe, H.; Kubota, M.; Chaen, H.; Fukuda, S.
    Construction and characterization of chimeric enzymes of kojibiose phosphorylase and trehalose phosphorylase from Thermoanaerobacter brockii (2006), Carbohydr. Res., 341, 2350-2359.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information chimeric phosphorylases are constructed of the kojibiose phosphorylase gene and the trehalose phosphorylase gene from Thermoanaerobacter brockii. Chimera V-III show not trehalose phosphorylase, but kojibiose phosphorylase activity, although only 125 amino acid residues in 785 residues of chimera V–III are from that of kojibiose phosphorylase. Chimera V-III have 1% of the specific activity of the wild-type kojibiose phosphorylase. The temperature profile and kinetic parameters of chimera V-III are remarkably changed as compared to those of the wild-type kojibiose phosphorylase. Chimera V–III protein exists as a monomer in solution, whereas wild-type kojibiose phosphorylase and trehalose phosphorylase are hexamer and dimer structures, respectively. The chimera acts on nigerose, sophorose and laminaribiose, in addition to kojibiose. Chimera V–III is also able to act on sophorose and laminaribiose in the absence of inorganic phosphate, and produces two trisaccharides, beta-D-glucosyl-(1,6)-laminaribiose and laminaritriose, from laminaribiose Thermoanaerobacter brockii

Organism

Organism UniProt Comment Textmining
Thermoanaerobacter brockii
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Purification (Commentary)

Purification (Comment) Organism
chimeric enzymes Thermoanaerobacter brockii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
kojibiose + phosphate
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Thermoanaerobacter brockii beta-D-glucose-1-phosphate + D-glucose
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