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serine hydroxymethyltransferase
Serine hydroxymethyltransferase (SHMT) is an enzyme () which plays an important role in cellular one-carbon pathways by catalyzing the reversible, simultaneous conversions of L-serine to glycine (retro-aldol cleavage) and tetrahydrofolate to 5,10-methylenetetrahydrofolate (hydrolysis). This reaction provides the largest part of the one-carbon units available to the cell.
== Isoforms ==
Bacteria such as ''Escherichia coli'' and ''Bacillus stearothermophilus'' have versions of this enzyme and there appear to be two isoforms of SHMT in mammals, one in the cytoplasm (cSHMT) and another in the mitochondria (mSHMT).〔 Plants may have an additional SHMT isoform within chloroplasts.
In mammals, the enzyme is a tetramer of four identical subunits of approximately 50,000 Daltons each. The intact holoenzyme has a molecular weight of approximately 200,000 Daltons and incorporates four molecules of pyridoxal phosphate (Vitamin B6) as a coenzyme.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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