Title | Discovery of sarcosine dimethylglycine methyltransferase from Galdieria sulphuraria. |
Publication Type | Journal Article |
Year of Publication | 2009 |
Authors | McCoy JG, Bailey LJ, Ng YHan, Bingman CA, Wrobel R, Weber APM, Fox BG, Phillips GN |
Journal | Proteins |
Volume | 74 |
Issue | 2 |
Pagination | 368-77 |
Date Published | 2009 Feb 1 |
ISSN | 1097-0134 |
Keywords | Algal Proteins, Crystallography, X-Ray, Enzyme Stability, Kinetics, Methyltransferases, Protein Folding, Protein Structure, Tertiary, Rhodophyta, Sarcosine, Sequence Alignment, Substrate Specificity, Temperature |
Abstract | 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 A, revealed a fold highly similar to that of mycolic acid synthases. The kcat and apparent K(M) values were 64.3 min(-1) and 2.0 mM for sarcosine and 85.6 min(-1) and 2.8 mM for dimethylglycine, respectively. Apparent K(M) values of S-adenosylmethionine were 144 and 150 microM for sarcosine and dimethylglycine, respectively, and the enzyme melting temperature was 61.1 degrees C. Modeling of cofactor binding in the active site based on the structure of methoxy mycolic acid synthase 2 revealed a number of conserved interactions within the active site. |
DOI | 10.1002/prot.22147 |
Alternate Journal | Proteins |
PubMed ID | 18623062 |
PubMed Central ID | PMC2742680 |
Grant List | 5T32HG002760 / HG / NHGRI NIH HHS / United States U54 GM074901 / GM / NIGMS NIH HHS / United States U54 GM074901-05 / GM / NIGMS NIH HHS / United States Y1-CO-1020 / CO / NCI NIH HHS / United States Y1-GM-1104 / GM / NIGMS NIH HHS / United States |