|Gene:||ppsA||Accession Numbers: EG10759 (MetaCyc), b1702, ECK1700|
Species: Escherichia coli K-12 substr. MG1655
Subunit composition of
phosphoenolpyruvate synthetase = [PpsA]2
phosphoenolpyruvate synthetase = PpsA
During growth on three-carbon substrates that require the gluconeogenesis pathway (such as lactate or pyruvate), phosphoenolpyruvate (PEP) synthetase provides the ability to generate phosphoenolpyruvate, which is required for the synthesis of precursor metabolites for cellular carbon compounds [Cooper67a].
The reaction is thought to proceed in two steps: hydrolysis of ATP, whereby the γ phosphate is released and the β phosphate is transiently attached to a histidine residue within the enzyme, followed by transfer of the phosphate residue to pyruvate, producing PEP [Berman70, Narindrasorasak77].
A regulatory mechanism of the enzymatic activity of PEP synthetase was recently identified. PEP synthetase regulatory protein (PSRP) catalyzes both the Pi-dependent activation and ADP/ATP-dependent inactivation of PEP synthetase. PEP synthetase is protected from inactivation by the presence of pyruvate [Burnell10].
PEP synthetase mutants do not grow on pyruvate, lactate or alanine as the sole source of carbon [Cooper65, Cooper67a, Brice67]. The wild-type expression level of ppsA appears to be suboptimal for growth on pyruvate [Chao93]. Expression of ppsA is increased by growth on acetate as the sole source of carbon [Oh00, Oh02, Peng03]. A ppsA mutant shows an increased lag time during the diauxic transition from growth on glucose to growth on acetate [Kao05]. A ppsA pckA double mutant does not grow on acetate [Oh02] or succinate [Goldie80] as the sole source of carbon.
|Map Position: [1,782,758 <- 1,785,136]|
Molecular Weight of Polypeptide: 87.435 kD (from nucleotide sequence), 84.0 kD (experimental) [Geerse89 ]
Unification Links: ASAP:ABE-0005678 , CGSC:367 , DIP:DIP-10552N , EchoBASE:EB0752 , EcoGene:EG10759 , EcoliWiki:b1702 , EcoO157Cyc:PPSA , ModBase:P23538 , OU-Microarray:b1702 , PortEco:ppsA , PR:PRO_000023582 , Pride:P23538 , Protein Model Portal:P23538 , RefSeq:NP_416217 , RegulonDB:EG10759 , SMR:P23538 , String:511145.b1702 , UniProt:P23538
Relationship Links: InterPro:IN-FAMILY:IPR000121 , InterPro:IN-FAMILY:IPR002192 , InterPro:IN-FAMILY:IPR006319 , InterPro:IN-FAMILY:IPR008279 , InterPro:IN-FAMILY:IPR013815 , InterPro:IN-FAMILY:IPR013816 , InterPro:IN-FAMILY:IPR015813 , InterPro:IN-FAMILY:IPR018274 , InterPro:IN-FAMILY:IPR023151 , Pfam:IN-FAMILY:PF00391 , Pfam:IN-FAMILY:PF01326 , Pfam:IN-FAMILY:PF02896 , Prosite:IN-FAMILY:PS00370 , Prosite:IN-FAMILY:PS00742
|Biological Process:||GO:0006094 - gluconeogenesis
GO:0006090 - pyruvate metabolic process [GOA01a]
GO:0016310 - phosphorylation [UniProtGOA11a, GOA01a]
|Molecular Function:||GO:0000287 - magnesium ion binding
GO:0008986 - pyruvate, water dikinase activity [GOA01, GOA01a, Cooper67a]
GO:0000166 - nucleotide binding [UniProtGOA11a]
GO:0003824 - catalytic activity [GOA01a]
GO:0005524 - ATP binding [UniProtGOA11a, GOA01a]
GO:0016301 - kinase activity [UniProtGOA11a, GOA01a]
GO:0016740 - transferase activity [UniProtGOA11a]
GO:0016772 - transferase activity, transferring phosphorus-containing groups [GOA01a]
GO:0046872 - metal ion binding [UniProtGOA11a]
|Cellular Component:||GO:0005829 - cytosol [DiazMejia09, Zhang07]|
|MultiFun Terms:||metabolism → central intermediary metabolism|
Enzymatic reaction of: phosphoenolpyruvate synthetase
Synonyms: pyruvate,water dikinase, phosphoenolpyruvate synthase, PEP synthase, ATP:pyruvate, water phosphotransferase
EC Number: 188.8.131.52
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.
The reaction is physiologically favored in the direction shown. [Cooper65]
In Pathways: superpathway of hexitol degradation (bacteria) , superpathway of N-acetylneuraminate degradation , superpathway of glycolysis and Entner-Doudoroff , superpathway of glycolysis, pyruvate dehydrogenase, TCA, and glyoxylate bypass , gluconeogenesis I , glycolysis II (from fructose 6-phosphate) , glycolysis I (from glucose 6-phosphate)
Only the enzyme from E. coli B has been biochemically characterized [Cook85, Cooper65, Cooper67a, Chulavatnatol73, Chulavatnatol73a, Berman70, Berman70a, Narindrasorasak77, Cooper67, Berman67]. The sequences of the E. coli B and K-12 enzymes are 99% identical.
Inhibitors (Unknown Mechanism): oxalate [Narindrasorasak78] , 2-oxoglutarate [Chulavatnatol73] , ADP [Chulavatnatol73] , oxaloacetate [Chulavatnatol73] , fluoride [Cooper65] , p-hydroxymercuribenzoate [Cooper69, Berman70] , AMP [Cooper69, Chulavatnatol73] , phosphoenolpyruvate [Cooper69, Chulavatnatol73]
pH(opt): 8-8.5 [Cooper67a]
|Chain||2 -> 792|
|Sequence-Conflict||194 -> 195|
|Sequence-Conflict||341 -> 360|
10/20/97 Gene b1702 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10759.
Berman70: Berman KM, Cohn M (1970). "Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent metal ions." J Biol Chem 245(20);5309-18. PMID: 4319237
Berman70a: Berman KM, Cohn M (1970). "Phosphoenolpyruvate synthetase. Partial reactions studied with adenosine triphosphate analogues and the inorganic phosphate-H2 18O exchange reaction." J Biol Chem 245(20);5319-25. PMID: 4319238
Brice67: Brice CB, Kornberg HL (1967). "Location of a gene specifying phosphopyruvate synthase activity on the genome of Escherichia coli, K12." Proc R Soc Lond B Biol Sci 168(12);281-92. PMID: 4383555
Burnell10: Burnell JN (2010). "Cloning and characterization of Escherichia coli DUF299: a bifunctional ADP-dependent kinase - phosphate-dependent pyrophosphorylase from bacteria." BMC Biochem 11(1);1. PMID: 20044937
Chulavatnatol73: Chulavatnatol M, Atkinson DE (1973). "Phosphoenolpyruvate synthetase from Escherichia coli. Effects of adenylate energy charge and modifier concentrations." J Biol Chem 248(8);2712-5. PMID: 4572511
Chulavatnatol73a: Chulavatnatol M, Atkinson DE (1973). "Kinetic competition in vitro between phosphoenolpyruvate synthetase and the pyruvate dehydrogenase complex from Escherichia coli." J Biol Chem 248(8);2716-21. PMID: 4572512
Cook85: Cook AG, Knowles JR (1985). "Phosphoenolpyruvate synthetase and pyruvate, orthophosphate dikinase: stereochemical consequences at both the beta-phospho and gamma-phospho groups of ATP." Biochemistry 24(1);51-8. PMID: 2986676
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
Geerse89: Geerse RH, van der Pluijm J, Postma PW (1989). "The repressor of the PEP:fructose phosphotransferase system is required for the transcription of the pps gene of Escherichia coli." Mol Gen Genet 218(2);348-52. PMID: 2674659
Goldie80: Goldie AH, Sanwal BD (1980). "Genetic and physiological characterization of Escherichia coli mutants deficient in phosphoenolpyruvate carboxykinase activity." J Bacteriol 141(3);1115-21. PMID: 6988403
Narindrasorasak77: Narindrasorasak S, Bridger WA (1977). "Phosphoenolpyruvate Synthetase of Escherichia coli. Molecular weight, subunit composition, and identification of phosphohistidine in phosphoenzyme intermediate." J Biol Chem 252(10):3121-3127.
Narindrasorasak78: Narindrasorasak S, Bridger WA (1978). "Probes of the structure of phosphoenolpyruvate synthetase: effects of a transition state analogue on enzyme conformation." Can J Biochem 56(8);816-9. PMID: 210911
Niersbach92: Niersbach M, Kreuzaler F, Geerse RH, Postma PW, Hirsch HJ (1992). "Cloning and nucleotide sequence of the Escherichia coli K-12 ppsA gene, encoding PEP synthase." Mol Gen Genet 1992;231(2);332-6. PMID: 1310524
Peng03: Peng L, Shimizu K (2003). "Global metabolic regulation analysis for Escherichia coli K12 based on protein expression by 2-dimensional electrophoresis and enzyme activity measurement." Appl Microbiol Biotechnol 61(2);163-78. PMID: 12655459
Phue05: Phue JN, Noronha SB, Hattacharyya R, Wolfe AJ, Shiloach J (2005). "Glucose metabolism at high density growth of E. coli B and E. coli K: differences in metabolic pathways are responsible for efficient glucose utilization in E. coli B as determined by microarrays and Northern blot analyses." Biotechnol Bioeng 90(7);805-20. PMID: 15806547
Zhang07: Zhang N, Chen R, Young N, Wishart D, Winter P, Weiner JH, Li L (2007). "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS." Proteomics 7(4);484-93. PMID: 17309111
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