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Pathway Description
Serine Metabolism
Saccharomyces cerevisiae
Metabolic Pathway
The biosynthesis of serine begins with 3-phospho-D-glycerate being metabolize into 3-phosphohydroxypyruvate through a 3-phosphoglycerate dehydrogenase. The resulting compound 3-phosphohydroxypyruvate is transaminated into 3-phospho-L-serine through a phosphoserine transaminase. This is followed by 3-phospho-L-serine being dephosphorylated through a phosphoserine phosphatase resulting in the release of a phosphate and Serine.
Serine can also be incorporated into the mitochondrion and then serine can then be used to synthesize glycine through a mitochondrial serine hydroxymethyltransferase. Glycine is then used to synthesize formic acid by first being metabolized into 5,10 methylene THF, which is transformed into a 5,10 methenyltetrahydrofolate , followed by an N10 formyl tetrahydrofolate and lastly formic acid, all through a mitochondrial C1-tetrahydrofolate synthase.
In the cytosol serine can either be degraded to synthesize glycine through a serine hydroxymethyltransferase or it can be degraded into 2-aminoprop-2-enoate. The latter compound can be spontaneously be converted first into 2-iminopropanoate and this compound is then converted into pyruvic acid.
References
Serine Metabolism References
Bornaes C, Petersen JG, Holmberg S: Serine and threonine catabolism in Saccharomyces cerevisiae: the CHA1 polypeptide is homologous with other serine and threonine dehydratases. Genetics. 1992 Jul;131(3):531-9.
Pubmed: 1628804
Albers E, Laize V, Blomberg A, Hohmann S, Gustafsson L: Ser3p (Yer081wp) and Ser33p (Yil074cp) are phosphoglycerate dehydrogenases in Saccharomyces cerevisiae. J Biol Chem. 2003 Mar 21;278(12):10264-72. doi: 10.1074/jbc.M211692200. Epub 2003 Jan 13.
Pubmed: 12525494
Jones EW and Fink GRĀ Regulation of amino acid and nucleotide biosynthesis in yeast. in The Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Expression, edited by Strathern JN, Jones EW and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press (1982) p.181-299
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