If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
|Superclasses:||Biosynthesis → Amino Acids Biosynthesis → Proteinogenic Amino Acids Biosynthesis → L-serine Biosynthesis|
Serine biosynthesis is a major metabolic pathway in E. coli. Its end product, 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, (S)-2-hydroxyglutarate reductase [multifunctional]. The second enzyme in the pathway, 3-phosphoserine aminotransferase, requires pyridoxal 5'-phosphate as a cofactor and is also required for the biosynthesis of pyridoxal 5'-phosphate itself. Thus the cell must ensure that the supply of pyridoxal 5'-phosphate 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, [ECOSAL]
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
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
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
Grant00: Grant GA, Xu XL, Hu Z (2000). "Removal of the tryptophan 139 side chain in Escherichia coli D-3-phosphoglycerate dehydrogenase produces a dimeric enzyme without cooperative effects." Arch Biochem Biophys 375(1);171-4. PMID: 10683264
Grant00a: Grant GA, Xu XL, Hu Z (2000). "Role of an interdomain Gly-Gly sequence at the regulatory-substrate domain interface in the regulation of Escherichia coli. D-3-phosphoglycerate dehydrogenase." Biochemistry 39(24);7316-9. PMID: 10852732
Grant01: Grant GA, Hu Z, Xu XL (2001). "Specific interactions at the regulatory domain-substrate binding domain interface influence the cooperativity of inhibition and effector binding in Escherichia coli D-3-phosphoglycerate dehydrogenase." J Biol Chem 276(2);1078-83. PMID: 11050089
Grant01a: Grant GA, Hu Z, Xu XL (2001). "Amino acid residue mutations uncouple cooperative effects in Escherichia coli D-3-phosphoglycerate dehydrogenase." J Biol Chem 276(21);17844-50. PMID: 11278587
Grant02: Grant GA, Hu Z, Xu XL (2002). "Cofactor binding to Escherichia coli D-3-phosphoglycerate dehydrogenase induces multiple conformations which alter effector binding." J Biol Chem 277(42);39548-53. PMID: 12183470
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