Serine hydroxymethyltransferase

IntroductionIntroduction

spinqualitylabelsall models Structure of Serine hydroxymethyltransferase isolated from Bacillus stearothermophilus Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Serine hydroxymethyltransferase (SHMT) is part of the pyridoxal phosphate (PLP)-dependent enzymes. Specifically, the enzyme belongs to the alpha-class. This enzyme is utilized mainly for two functions. First, the enzyme catalyzes the reversible conversion of serine to glycine. Chemically speaking, the enzyme performs a retro-aldol cleavage. Second, the enzyme catalyzes the reversible conversion of tetrahydrofolate to 5,10-methylene tetrahydrofolate. There appear to be multiple isoforms of the enzyme in bacteria. Serine hydroxymethyltransferase isoforms have namely been identified from Escherichia coli and Bacillus stearothermophilus. In mammals, there are two separate isoforms of SHMT in the cytoplasm and the mitochondria. In plants, there is an additional SHMT isoform found within the chloroplast. The diverse presence of serine hydroxymethyltransferase is in part because of the importance of 5,10-methylene tetrahydrofolate. This intermediate is important for the synthesis of the essential biomolecules purine, thymidine, choline, and methionine. The enzyme monomer fold is comprised of the c-terminal domain and the N-Terminal Domain. The C-terminal domain folds into an

StructureStructure

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