Glycine, Serine and Threonine Metabolism in T. maritima

Description:

T. maritima (Thermotoga maritima), is an anerobic, Gram-negative, rod-shaped bacterium which usually grows singly or in pairs. The organism has an optimum growth temperature of 80 degrees centigrade. T. maritima metabolizes many simple and complex carbohydrates, keto-acids, etc. to fuels such as Hydrogen. The metabolism of amino acids like Glycine, Serine and Threonine acts as a source of carbon and energy for T. maritima by the conversion of amino acids to keto-acids and carbohydrates (Ref...

References:

Physics and evolution of thermophilic adaptation.
Berezovsky IN, Shakhnovich EI.
Proc. Natl. Acad. Sci. U S A. 2005 Sep 6;102(36):12742-7.
Crystal structure of T-protein of the glycine cleavage system. Cofactor binding, insights into H-protein recognition, and molecular basis for understanding nonketotic hyperglycinemia.
Lee HH, Kim do J, Ahn HJ, Ha JY, Suh SW.
J. Biol. Chem. 2004 Nov 26;279(48):50514-23.
Structural genomics of thermotoga maritima proteins shows that contact order is a major determinant of protein thermostability.
Robinson-Rechavi M, Godzik A.
Structure. 2005 Jun;13(6):857-60.
Gene transfer and genome plasticity in Thermotoga maritima, a model hyperthermophilic species.
Mongodin EF, Hance IR, Deboy RT, Gill SR, Daugherty S, Huber R, Fraser CM, Stetter K, Nelson KE.
J. Bacteriol. 2005 Jul;187(14):4935-44.

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Pathways

Glycine, Serine and Threonine Metabolism in T. maritima

Description:

References:

Physics and evolution of thermophilic adaptation.

Crystal structure of T-protein of the glycine cleavage system. Cofactor binding, insights into H-protein recognition, and molecular basis for understanding nonketotic hyperglycinemia.

Structural genomics of thermotoga maritima proteins shows that contact order is a major determinant of protein thermostability.

Gene transfer and genome plasticity in Thermotoga maritima, a model hyperthermophilic species.

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Institutional License

Pathways

Glycine, Serine and Threonine Metabolism in T. maritima

Description:

References:

Physics and evolution of thermophilic adaptation.

Crystal structure of T-protein of the glycine cleavage system. Cofactor binding, insights into H-protein recognition, and molecular basis for understanding nonketotic hyperglycinemia.

Structural genomics of thermotoga maritima proteins shows that contact order is a major determinant of protein thermostability.

Gene transfer and genome plasticity in Thermotoga maritima, a model hyperthermophilic species.

Databases

Tools

Institutional License

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