Abstract
Serine hydroxymethyltransferase (EC 2.1.2.1) is a pyridoxalphosphate containing enzyme which, among other reactions, catalyzes the tetrahydrofolate-dependent interconversion of serine and glycine, thus representing the major source of one-carbon groups required for the biosynthesis of several cell components1. Both cytosolic and mitochondrial forms exist in eukaryotic cells and preliminary sequence studies have demonstrated that these two isoenzymes are homologous proteins2. Cytosolic serine hydroxymethyltransferase from rabbit liver is the enzyme form by far the best characterized from the functional and spectroscopic point of view1. As far as the protein moiety is concerned, this enzyme is a tetramer of identical subunits with a molecular weight of about 215,000. We initiated the determination of its primary structure by purifying and analysing two active-site peptides3,4. Additional sequence information has been accumulated after analysis of tryptic, chymotryptic and, now, CNBr peptides.
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© 1987 Plenum Press, New York
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Barra, D., Martini, F., Angelaccio, S., Pascarella, S., Bossa, F., Schirch, L. (1987). Primary Structure Studies on Serine Hydroxymethyltransferase. In: L’Italien, J.J. (eds) Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1787-6_78
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DOI: https://doi.org/10.1007/978-1-4613-1787-6_78
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