期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 74, 期 2, 页码 368-377出版社
WILEY
DOI: 10.1002/prot.22147
关键词
betaine synthesis; structural genomics; thermophile; osmoregulation
资金
- U.S. Department of Energy [W-31-109-FNG-38]
- National Cancer Instialte [Y1-CO-1020]
- National Institute of General Medical Science [Y1-GM-1104]
- National Institutes of Health [U54 GM074901]
- NHGRI training grant [5T32HG002760]
- National Science Foundations [MCB-0316232]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0843239] Funding Source: National Science Foundation
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 angstrom, revealed a fold highly similar to that of mycolic acid synthases. The k(cat), and apparent Km 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 Km values of S-adenosylmethionine were 144 and 150 mu M 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.
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