Discovery of sarcosine dimethylglycine methyltransferase from Galdieria sulphuraria

An enzyme with sarcosine dimethylglycine methyltransferase (SDMT) activity has been identified in the thermophilic eukaryote, Galdieria sulphuraria. The crystal structure of the enzyme, solved to a resolution of 1.95 Å, revealed a fold highly similar to that of mycolic acid synthases. The kcat and a...

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Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2009-02, Vol.74 (2), p.368-377
Hauptverfasser:	McCoy, Jason G., Bailey, Lucas J., Ng, Yi Han, Bingman, Craig A., Wrobel, Russell, Weber, Andreas P. M., Fox, Brian G., Phillips Jr, George N.
Format:	Artikel
Sprache:	eng
Schlagworte:	Algal Proteins - chemistry Algal Proteins - isolation & purification Algal Proteins - metabolism betaine synthesis Crystallography, X-Ray Enzyme Stability Kinetics Methyltransferases - chemistry Methyltransferases - isolation & purification Methyltransferases - metabolism osmoregulation Protein Folding Protein Structure, Tertiary Rhodophyta - enzymology Sarcosine - analogs & derivatives Sarcosine - metabolism Sequence Alignment structural genomics Substrate Specificity Temperature thermophile
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