This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
|Superclasses:||Biosynthesis → Amino Acids Biosynthesis → Individual Amino Acids Biosynthesis → Serine Biosynthesis|
About This Pathway
Serine biosynthesis is a major metabolic pathway in Escherichia coli K-12. Its end product, L-serine, is not only used in protein synthesis, but also as a precursor for the biosynthesis of glycine, cysteine, tryptophan, and phospholipids. In addition, it directly or indirectly serves as a source of one-carbon units for the biosynthesis of various compounds.
Regulation of the pathway is mainly accomplished by feedback inhibition of the enzyme that catalyzes the first committed step, D-3-phosphoglycerate dehydrogenase. The second enzyme in the pathway, 3-phosphoserine aminotransferase, requires pyridoxal 5'-phosphate (PLP) as a cofactor and is also required for the biosynthesis of PLP itself. Thus the cell must ensure that the supply of PLP is adequate. Little biochemical work has been done on the final enzyme of the pathway, phosphoserine phosphatase.
Review: Stauffer, G., Regulation of Serine, Glycine, and One-Carbon Biosynthesis. Module 220.127.116.11, in [ECOSAL].
Serine Biosynthesis in Plants
Serine biosynthesis in plants proceeds by two pathways, the so called phosphorylated pathway and the glycolate pathway. In the phosphorylated pathway (depicted here), serine is derived from 3-phosphoglycerate, an intermediate of glycolysis. This pathway also operates in bacteria, yeast, and animals. In the glycolate pathway, which is part of photorespiration (photorespiration), serine is derived from glycolate via glycine. The glycolate pathway dominates in the photosynthetic tissues. Most of the serine produced in this pathway continues with the photorespiration pathway and is returned to Calvin cycle via hydroxypyruvate and glycerate. The phosphorylated pathway is thought to contribute to serine biosynthesis in the dark and in non-photosynthetic tissues. Genes of the phosphorylated pathway are upregulated by high salinity, flood and cold. It indicates that the phosphorylated pathway is also important in supplying serine under environmental stresses.
AlRabiee96: Al-Rabiee R, Zhang Y, Grant GA (1996). "The mechanism of velocity modulated allosteric regulation in D-3-phosphoglycerate dehydrogenase. Site-directed mutagenesis of effector binding site residues." J Biol Chem 271(38);23235-8. PMID: 8798520
Baek00: Baek JY, Jun DY, Taub D, Kim YH (2000). "Assignment of human 3-phosphoglycerate dehydrogenase (PHGDH) to human chromosome band 1p12 by fluorescence in situ hybridization." Cytogenet Cell Genet 89(1-2);6-7. PMID: 10894924
Baek03: Baek JY, Jun DY, Taub D, Kim YH (2003). "Characterization of human phosphoserine aminotransferase involved in the phosphorylated pathway of L-serine biosynthesis." Biochem J 373(Pt 1);191-200. PMID: 12633500
Burton08: Burton RL, Hanes JW, Grant GA (2008). "A stopped flow transient kinetic analysis of substrate binding and catalysis in Escherichia coli D-3-phosphoglycerate dehydrogenase." J Biol Chem 283(44);29706-14. PMID: 18776184
Burton09: Burton RL, Chen S, Xu XL, Grant GA (2009). "Transient kinetic analysis of the interaction of L-serine with Escherichia coli D-3-phosphoglycerate dehydrogenase reveals the mechanism of V-type regulation and the order of effector binding." Biochemistry 48(51);12242-51. PMID: 19924905
Clarke73: Clarke SJ, Low B, Konigsberg WH (1973). "Close linkage of the genes serC (for phosphohydroxy pyruvate transaminase) and serS (for seryl-transfer ribonucleic acid synthetase) in Escherichia coli K-12." J Bacteriol 113(3);1091-5. PMID: 4570768
Collet97: Collet JF, Gerin I, Rider MH, Veiga-da-Cunha M, Van Schaftingen E (1997). "Human L-3-phosphoserine phosphatase: sequence, expression and evidence for a phosphoenzyme intermediate." FEBS Lett 408(3);281-4. PMID: 9188776
Collet98: Collet JF, Stroobant V, Pirard M, Delpierre G, Van Schaftingen E (1998). "A new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif." J Biol Chem 273(23);14107-12. PMID: 9603909
Dey07: Dey S, Hu Z, Xu XL, Sacchettini JC, Grant GA (2007). "The effect of hinge mutations on effector binding and domain rotation in Escherichia coli D-3-phosphoglycerate dehydrogenase." J Biol Chem 282(25);18418-26. PMID: 17459882
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Drewke96: Drewke C, Klein M, Clade D, Arenz A, Muller R, Leistner E (1996). "4-O-phosphoryl-L-threonine, a substrate of the pdxC(serC) gene product involved in vitamin B6 biosynthesis." FEBS Lett 1996;390(2);179-82. PMID: 8706854
Duncan86: Duncan K, Coggins JR (1986). "The serC-aro A operon of Escherichia coli. A mixed function operon encoding enzymes from two different amino acid biosynthetic pathways." Biochem J 1986;234(1);49-57. PMID: 3518706
Showing only 20 references. To show more, press the button "Show all references".
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493