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Gene Review:

TM0025 - beta-glucosidase

Thermotoga maritima MSB8

Liebl, W. et al., Zechel, D.L. et al., Gloster, T.M. et al., Bauer, M.W. et al., Goyal, K. et al.

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Disease relevance of TM0025

Here, the binding of 1-deoxynojirimycin and (+)-isofagomine to the "family GH-1" beta-glucosidase of Thermotoga maritima is investigated by kinetic analysis, isothermal titration calorimetry, and X-ray crystallography [1].
In contrast, the beta-glucosidase from Cellvibrio gilvus is mesophilic (35 degrees C) and displays no such transglycosylation activity [2].
The T. maritima beta-glucosidase (BglA) was overexpressed in E. coli at a level comprising approximately 15-20% of soluble cellular protein [3].

High impact information on TM0025

X-ray structures with both a beta-glucosidase, at 2 A resolution, and an endoglucanase at atomic (approximately 1 A) resolution reveal similar interactions between the tetrahydrooxazine inhibitor and both enzymes [4].
The kinetic differences between the two enzymes suggest that, unlike the beta-glucosidase, the primary role of the beta-mannosidase may not be disaccharide hydrolysis [5].
Comparative amino acid sequence analysis of Thermotoga maritima beta-glucosidase (BglA) deduced from the nucleotide sequence of the gene indicates distant relationship between beta-glucosidases of the BGA family and other families of beta-1,4-glycosyl hydrolases [3].
Based on its amino acid sequence, as deduced from the nucleotide sequence of the gene, BglA can be classified as a broad-specificity beta-glucosidase and as a member of the beta-glucosidase family BGA, in agreement with the results of enzymatic characterization of the recombinant protein [3].

Associations of TM0025 with chemical compounds

Given that these results contradict earlier proposals that the binding of racemic isofagomine to sweet almond beta-glucosidase was entropically driven (Bülow, A. et al. J. Am. Chem. Soc. 2000, 122, 8567-8568), we reinvestigated the binding of 1-deoxynojirimycin and isofagomine to the sweet almond enzyme [1].

Analytical, diagnostic and therapeutic context of TM0025

Kinetic analyses reveal the pH dependence of kcat/Km and 1/Ki with both enzyme systems, and isothermal titration calorimetry unveils the enthalpic and entropic contributions to beta-glucosidase inhibition [4].
Comparison of a beta-glucosidase and a beta-mannosidase from the hyperthermophilic archaeon Pyrococcus furiosus. Purification, characterization, gene cloning, and sequence analysis [5].

References

Iminosugar glycosidase inhibitors: structural and thermodynamic dissection of the binding of isofagomine and 1-deoxynojirimycin to beta-glucosidases. Zechel, D.L., Boraston, A.B., Gloster, T., Boraston, C.M., Macdonald, J.M., Tilbrook, D.M., Stick, R.V., Davies, G.J. J. Am. Chem. Soc. (2003) [Pubmed]
Enhancement of transglycosylation activity by construction of chimeras between mesophilic and thermophilic beta-glucosidase. Goyal, K., Jo Kim, B., Kim, J.D., Kim, Y.K., Kitaoka, M., Hayashi, K. Arch. Biochem. Biophys. (2002) [Pubmed]
Comparative amino acid sequence analysis of Thermotoga maritima beta-glucosidase (BglA) deduced from the nucleotide sequence of the gene indicates distant relationship between beta-glucosidases of the BGA family and other families of beta-1,4-glycosyl hydrolases. Liebl, W., Gabelsberger, J., Schleifer, K.H. Mol. Gen. Genet. (1994) [Pubmed]
Structural, thermodynamic, and kinetic analyses of tetrahydrooxazine-derived inhibitors bound to beta-glucosidases. Gloster, T.M., Macdonald, J.M., Tarling, C.A., Stick, R.V., Withers, S.G., Davies, G.J. J. Biol. Chem. (2004) [Pubmed]
Comparison of a beta-glucosidase and a beta-mannosidase from the hyperthermophilic archaeon Pyrococcus furiosus. Purification, characterization, gene cloning, and sequence analysis. Bauer, M.W., Bylina, E.J., Swanson, R.V., Kelly, R.M. J. Biol. Chem. (1996) [Pubmed]

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