IntroductionIntroduction
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"
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