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Gene Review:

TM1414 - beta-fructosidase

Thermotoga maritima MSB8

Alberto, F. et al., Nagem, R.A. et al., Liebl, W. et al.

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Disease relevance of TM1414

The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases [1].
Analysis of the gene for beta-fructosidase (invertase, inulinase) of the hyperthermophilic bacterium Thermotoga maritima, and characterisation of the enzyme expressed in Escherichia coli [2].

High impact information on TM1414

Thermotoga maritima invertase (beta-fructosidase) hydrolyzes sucrose to release fructose and glucose, which are major carbon and energy sources for both prokaryotes and eukaryotes [1].
Its structural architecture is very similar to that of another member of glycoside hydrolase family 32, invertase (beta-fructosidase) from Thermotoga maritima, determined recently by X-ray crystallography The exo-inulinase is a glycoprotein containing five N-linked oligosaccharides [3].

References

The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases. Alberto, F., Bignon, C., Sulzenbacher, G., Henrissat, B., Czjzek, M. J. Biol. Chem. (2004) [Pubmed]
Analysis of the gene for beta-fructosidase (invertase, inulinase) of the hyperthermophilic bacterium Thermotoga maritima, and characterisation of the enzyme expressed in Escherichia coli. Liebl, W., Brem, D., Gotschlich, A. Appl. Microbiol. Biotechnol. (1998) [Pubmed]
Crystal structure of exo-inulinase from Aspergillus awamori: the enzyme fold and structural determinants of substrate recognition. Nagem, R.A., Rojas, A.L., Golubev, A.M., Korneeva, O.S., Eneyskaya, E.V., Kulminskaya, A.A., Neustroev, K.N., Polikarpov, I. J. Mol. Biol. (2004) [Pubmed]

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