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Literature summary for 3.2.1.2 extracted from

  • Wang, J.H.; Tsai, M.Y.; Lee, G.C.; Shaw, J.F.
    Construction of a recombinant thermostable beta-amylase-trehalose synthase bifunctional enzyme for facilitating the conversion of starch to trehalose (2007), J. Agric. Food Chem., 55, 1256-1263.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
a fusion gene that encodes a polypeptide of 1495 amino acids is constructed from the beta-amylase gene of Clostridium thermosulfurogenes and trehalose synthase gene of Thermus thermophilus. The fused gene is overexpressed in Escherichia coli, and a recombinant bifunctional fusion protein with beta-amylase at the N-terminal or C-terminal of trehalose synthase having both beta-amylase and trehalose synthase activities with an apparent molecular mass of 164000 Da is obtained Thermoanaerobacterium thermosulfurigenes

Protein Variants

Protein Variants Comment Organism
additional information a fusion gene that encodes a polypeptide of 1495 amino acids is constructed from the beta-amylase (BA) gene of Clostridium thermosulfurogenes and trehalose synthase (TS) gene of Thermus thermophilus. The fused gene is overexpressed in Escherichia coli, and a recombinant bifunctional fusion protein with beta-amylase at the N-terminal (BATS) or C-terminal (TSBA) of trehalose synthase having both beta-amylase and trehalose synthase activities with an apparent molecular mass of 164000 Da is obtained. BATS or TSBA catalyzes the sequential reaction in which maltose is formed from starch and then is converted into trehalose. The Km values of the BATS and TSBA fusion enzymes for the reaction from starch to trehalose are smaller than those of an equimolar mixture of BA and TS (BA/TS). The kcat value of BATS approximates that of the BA/TS mixture, but that of TSBA exceedes it. TSBA shows much higher sequential catalytic efficiency than the separately expressed BA/TS mixture. The catalytic efficiency of TSBA or BATS is 3.4 or 2.4times higher, respectively, than that of a mixture of individual enzymes. The thermal stability readings of the recombinant fusion enzymes BATS and TSBA are better than that of the mixture of individual recombinant enzymes Thermoanaerobacterium thermosulfurigenes

Organism

Organism UniProt Comment Textmining
Thermoanaerobacterium thermosulfurigenes
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Purification (Commentary)

Purification (Comment) Organism
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Thermoanaerobacterium thermosulfurigenes