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Escherichia coli K-12 substr. MG1655 Pathway: superpathway of L-aspartate and L-asparagine biosynthesis

Pathway diagram: superpathway of L-aspartate and L-asparagine biosynthesis

If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Locations of Mapped Genes:

Schematic showing all replicons, marked with selected genes

Genetic Regulation Schematic

Genetic regulation schematic for superpathway of L-aspartate and L-asparagine biosynthesis

Synonyms: Interconversion of L-aspartate and L-asparagine

Superclasses: BiosynthesisAmino Acids Biosynthesis
Metabolic Clusters

Aspartate undergoes a number of reactions that are not in any linear order. One reaction converts the TCA intermediate fumarate to aspartate. Another reaction irreversibly converts aspartate to asparagine. A third reaction facilitates reversible interconversion of aspartate and asparargine. In E. coli aspartate participates in at least two metabolic processes: the regeneration of oxaloacetate as amino-acceptor for enabling growth on glutamate, and the formation of fumarate and succinate during anaerobic growth on glucose. [Guest84, Falzone88]

In addition to its role in synthesis of asparagine, aspartate serves as a precursor in synthesis of lysine, methionine and threonine, plus the pyrimidines. Also the intermediate argininosuccinate hydrolyses to give citrulline and aspartate.

Subpathways: L-glutamate degradation II, L-aspartate biosynthesis, L-asparagine biosynthesis II


Falzone88: Falzone CJ, Karsten WE, Conley JD, Viola RE (1988). "L-aspartase from Escherichia coli: substrate specificity and role of divalent metal ions." Biochemistry 1988;27(26);9089-93. PMID: 2853974

Guest84: Guest JR, Roberts RE, Wilde RJ (1984). "Cloning of the aspartase gene (aspA) of Escherichia coli." J Gen Microbiol 1984;130 ( Pt 5);1271-8. PMID: 6088667

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Almo94: Almo SC, Smith DL, Danishefsky AT, Ringe D (1994). "The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli." Protein Eng 7(3);405-12. PMID: 7909946

Asano05: Asano Y, Kira I, Yokozeki K (2005). "Alteration of substrate specificity of aspartase by directed evolution." Biomol Eng 22(1-3);95-101. PMID: 15857789

Aung00: Aung HP, Bocola M, Schleper S, Rohm KH (2000). "Dynamics of a mobile loop at the active site of Escherichia coli asparaginase." Biochim Biophys Acta 1481(2);349-59. PMID: 11018727

Bahreini14: Bahreini E, Aghaiypour K, Abbasalipourkabir R, Goodarzi MT, Saidijam M, Safavieh SS (2014). "An optimized protocol for overproduction of recombinant protein expression in Escherichia coli." Prep Biochem Biotechnol 44(5);510-28. PMID: 24219068

Birolo95: Birolo L, Sandmeier E, Christen P, John RA (1995). "The roles of Tyr70 and Tyr225 in aspartate aminotransferase assessed by analysing the effects of mutations on the multiple reactions of the substrate analogue serine o-sulphate." Eur J Biochem 232(3);859-64. PMID: 7588727

Birolo99: Birolo L, Malashkevich VN, Capitani G, De Luca F, Moretta A, Jansonius JN, Marino G (1999). "Functional and structural analysis of cis-proline mutants of Escherichia coli aspartate aminotransferase." Biochemistry 38(3);905-13. PMID: 9893985

Boehlein94: Boehlein SK, Richards NG, Schuster SM (1994). "Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad." J Biol Chem 269(10);7450-7. PMID: 7907328

Bonner90: Bonner CA, Fischer RS, Ahmad S, Jensen RA (1990). "Remnants of an ancient pathway to L-phenylalanine and L-tyrosine in enteric bacteria: evolutionary implications and biotechnological impact." Appl Environ Microbiol 56(12);3741-7. PMID: 2082822

Bonthron90: Bonthron DT (1990). "L-asparaginase II of Escherichia coli K-12: cloning, mapping and sequencing of the ansB gene." Gene 1990;91(1);101-5. PMID: 2144836

Borek00: Borek D, Jaskolski M (2000). "Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome." Acta Crystallogr D Biol Crystallogr 2000;56 ( Pt 11);1505-7. PMID: 11053866

Borek04: Borek D, Michalska K, Brzezinski K, Kisiel A, Podkowinski J, Bonthron DT, Krowarsch D, Otlewski J, Jaskolski M (2004). "Expression, purification and catalytic activity of Lupinus luteus asparagine beta-amidohydrolase and its Escherichia coli homolog." Eur J Biochem 271(15);3215-26. PMID: 15265041

Borek14: Borek D, Kozak M, Pei J, Jaskolski M (2014). "Crystal structure of active site mutant of antileukemic L-asparaginase reveals conserved zinc-binding site." FEBS J 281(18);4097-111. PMID: 25040257

BRENDA14: BRENDA team (2014). Imported from BRENDA version existing on Aug 2014.

Burland93: Burland V, Plunkett G, Daniels DL, Blattner FR (1993). "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Genomics 1993;16(3);551-61. PMID: 7686882

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Cedar67: Cedar H, Schwartz JH (1967). "Localization of the two-L-asparaginases in anaerobically grown Escherichia coli." J Biol Chem 242(16);3753-5. PMID: 4962587

Cedar68: Cedar H, Schwartz JH (1968). "Production of L-asparaginase II by Escherichia coli." J Bacteriol 96(6);2043-8. PMID: 4881701

Cedar69: Cedar H, Schwartz JH (1969). "The asparagine synthetase of Escherhic coli. I. Biosynthetic role of the enzyme, purification, and characterization of the reaction products." J Biol Chem 1969;244(15);4112-21. PMID: 4895361

Cedar69a: Cedar H, Schwartz JH (1969). "The asparagine synthetase of Escherichia coli. II. Studies on mechanism." J Biol Chem 1969;244(15);4122-7. PMID: 4895362

Chao99: Chao YP, Lai ZJ, Chen P, Chern JT (1999). "Enhanced conversion rate of L-phenylalanine by coupling reactions of aminotransferases and phosphoenolpyruvate carboxykinase in Escherichia coli K-12." Biotechnol Prog 15(3);453-8. PMID: 10356262

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by Pathway Tools version 19.5 (software by SRI International) on Tue May 3, 2016, biocyc14.