Serine hydroxymethyltransferase: Difference between revisions
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[[Serine hydroxymethyltransferase]] (SHMT) is part of the pyridoxal phosphate (PLP)-dependent enzymes. The enzyme is broadly classified as a transferase enzyme. Transferase enzymes primarily work by catalyzing the transfer of a specific functional group from one molecule to another. For example, a methyl group may need to be transferred from one molecule to another in ''vivo''. The transferase enzymes will catalyze the transfer of this methyl group. | [[Serine hydroxymethyltransferase]] (SHMT) is part of the pyridoxal phosphate (PLP)-dependent enzymes. The enzyme is broadly classified as a transferase enzyme. Transferase enzymes primarily work by catalyzing the transfer of a specific functional group from one molecule to another. For example, a methyl group may need to be transferred from one molecule to another in ''vivo''. The transferase enzymes will catalyze the transfer of this methyl group. | ||
Specifically, the enzyme belongs to the alpha-class. This enzyme is utilized mainly for two functions. First, the enzyme catalyzes the reversible conversion of L-serine to L-glycine. Second, the enzyme catalyzes the reversible conversion of tetrahydrofolate to 5,10-methylene tetrahydrofolate. The mechanism for the interconversion of both molecules is shown below. [[Image: | Specifically, the enzyme belongs to the alpha-class. This enzyme is utilized mainly for two functions. First, the enzyme catalyzes the reversible conversion of L-serine to L-glycine. Second, the enzyme catalyzes the reversible conversion of tetrahydrofolate to 5,10-methylene tetrahydrofolate. The mechanism for the interconversion of both molecules is shown below. [[Image:SHMT Function.png|thumb|left|260px| Enzymatic Function of SHMT]] | ||
===Diversity/Importance=== | ===Diversity/Importance=== | ||
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. Serine hydroxymethyltransferase plays a very important role in the Smith-Magneis syndrome (SMS). SHMT is also being studied in the field of anti-cancer and anti-microbials drugs. | 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. Serine hydroxymethyltransferase plays a very important role in the Smith-Magneis syndrome (SMS). SHMT is also being studied in the field of anti-cancer and anti-microbials drugs. | ||