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

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

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.

Synonyms: Interconversion of L-aspartate and L-asparagine

Superclasses: BiosynthesisAmino Acids Biosynthesis
Metabolic Clusters

Some taxa known to possess this pathway include : Escherichia coli K-12 substr. MG1655

Expected Taxonomic Range: Bacteria

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 Escherichia coli aspartase 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]

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

Unification Links: EcoCyc:ASPASN-PWY


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

Asai95: Asai Y, Inui M, Vertes A, Kobayashi M, Yukawa H (1995). "Cloning and sequence determination of the aspartase-encoding gene from Brevibacterium flavum MJ233." Gene 158(1);87-90. PMID: 7789816

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

Birolo00: Birolo L, Tutino ML, Fontanella B, Gerday C, Mainolfi K, Pascarella S, Sannia G, Vinci F, Marino G (2000). "Aspartate aminotransferase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125. Cloning, expression, properties, and molecular modelling." Eur J Biochem 267(9);2790-802. PMID: 10785402

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, Walworth ES, Schuster SM (1994). "Arginine 30 and asparagine 74 have functional roles in the glutamine dependent activities of Escherichia coli asparagine synthetase B." J Biol Chem 269(43);26789-95. PMID: 7929415

Boehlein94a: 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

Boehlein96: Boehlein SK, Schuster SM, Richards NG (1996). "Glutamic acid gamma-monohydroxamate and hydroxylamine are alternate substrates for Escherichia coli asparagine synthetase B." Biochemistry 35(9);3031-7. PMID: 8608142

Boehlein97: Boehlein SK, Walworth ES, Richards NG, Schuster SM (1997). "Mutagenesis and chemical rescue indicate residues involved in beta-aspartyl-AMP formation by Escherichia coli asparagine synthetase B." J Biol Chem 272(19);12384-92. PMID: 9139684

Boehlein97a: Boehlein SK, Walworth ES, Schuster SM (1997). "Identification of cysteine-523 in the aspartate binding site of Escherichia coli asparagine synthetase B." Biochemistry 36(33);10168-77. PMID: 9254614

Boehlein98: Boehlein SK, Stewart JD, Walworth ES, Thirumoorthy R, Richards NG, Schuster SM (1998). "Kinetic mechanism of Escherichia coli asparagine synthetase B." Biochemistry 37(38);13230-8. PMID: 9748330

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.

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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