Premium
Discovery of sarcosine dimethylglycine methyltransferase from Galdieria sulphuraria
Author(s) -
McCoy Jason G.,
Bailey Lucas J.,
Ng Yi Han,
Bingman Craig A.,
Wrobel Russell,
Weber Andreas P. M.,
Fox Brian G.,
Phillips George N.
Publication year - 2008
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.22147
Subject(s) - sarcosine , enzyme , biochemistry , chemistry , methyltransferase , stereochemistry , biology , amino acid , methylation , glycine , dna
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 k cat and apparent K M values were 64.3 min −1 and 2.0 m M 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 μ M for sarcosine and dimethylglycine, respectively, and the enzyme melting temperature was 61.1°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. Proteins 2009. © 2008 Wiley‐Liss, Inc.