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: L-aspartate biosynthesis and degradation
|Superclasses:||Biosynthesis → Amino Acids Biosynthesis → Proteinogenic Amino Acids Biosynthesis → L-aspartate Biosynthesis|
L-aspartate is synthesized from and degraded to oxaloacetate, an intermediate of the TCA cycle I (prokaryotic), by a reversible transamination reaction with L-glutamate (for the degradation of aspartate, see L-aspartate degradation I). This pathway is common in both prokaryotes and eukaryotes, and provides a link between amino acid and carbohydrate metabolism.
oxaloacetate, which is consumed in this pathway, is replenished from the TCA cycle I (prokaryotic) and from the pyruvate carboxylase reaction in both bacteria and eukaryotes, and from phosphoenolpyruvate carboxylase in some bacteria [Gottschalk86].
In Escherichia coli K-12 the aspartate aminotransferase, PLP-dependent, encoded by the aspC gene, is the principal transaminase that catalyzes this reaction, although tyrosine aminotransferase, which is encoded by tyrB, also catalyzes it. Null mutations in aspC do not confer aspartate auxotrophy, while null mutations in both aspC and tyrB do.
In addition to being a constituent of proteins, L-aspartate is also a precursor for the biosynthesis of many other compounds including L-lysine, L-threonine, L-methionine and NAD+ (see aspartate superpathway).
Superpathways: superpathway of L-methionine biosynthesis (by sulfhydrylation) , superpathway of L-methionine biosynthesis (transsulfuration) , Methanobacterium thermoautotrophicum biosynthetic metabolism , superpathway of L-threonine biosynthesis , superpathway of L-isoleucine biosynthesis I , superpathway of L-aspartate and L-asparagine biosynthesis , superpathway of L-lysine, L-threonine and L-methionine biosynthesis I , aspartate superpathway
Variants: L-glutamate degradation II
Unification Links: EcoCyc:ASPARTATESYN-PWY
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
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
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
BousquetLemerci90: Bousquet-Lemercier B, Pol S, Pave-Preux M, Hanoune J, Barouki R (1990). "Properties of human liver cytosolic aspartate aminotransferase mRNAs generated by alternative polyadenylation site selection." Biochemistry 29(22);5293-9. PMID: 1974457
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
Chow04: Chow MA, McElroy KE, Corbett KD, Berger JM, Kirsch JF (2004). "Narrowing substrate specificity in a directly evolved enzyme: the A293D mutant of aspartate aminotransferase." Biochemistry 43(40);12780-7. PMID: 15461450
DAniello05a: D'Aniello A, Fisher G, Migliaccio N, Cammisa G, D'Aniello E, Spinelli P (2005). "Amino acids and transaminases activity in ventricular CSF and in brain of normal and Alzheimer patients." Neurosci Lett 388(1);49-53. PMID: 16039064
Danishefsky91: Danishefsky AT, Onnufer JJ, Petsko GA, Ringe D (1991). "Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase." Biochemistry 1991;30(7);1980-5. PMID: 1993208
Deu07: Deu E, Kirsch JF (2007). "Cofactor-directed reversible denaturation pathways: the cofactor-stabilized Escherichia coli aspartate aminotransferase homodimer unfolds through a pathway that differs from that of the apoenzyme." Biochemistry 46(19);5819-29. PMID: 17441730
Deu09: Deu E, Dhoot J, Kirsch JF (2009). "The partially folded homodimeric intermediate of Escherichia coli aspartate aminotransferase contains a "molten interface" structure." Biochemistry 48(2);433-41. PMID: 19099423
Felbeck80: Felbeck H, Grieshaber MK (1980). "Investigations on some enzymes involved in the anaerobic metabolism of amino acids of Arenicola marina L." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 66(2);205-213.
Fernandez12: Fernandez FJ, de Vries D, Pena-Soler E, Coll M, Christen P, Gehring H, Vega MC (2012). "Structure and mechanism of a cysteine sulfinate desulfinase engineered on the aspartate aminotransferase scaffold." Biochim Biophys Acta 1824(2);339-49. PMID: 22138634
Fotheringham86: Fotheringham IG, Dacey SA, Taylor PP, Smith TJ, Hunter MG, Finlay ME, Primrose SB, Parker DM, Edwards RM (1986). "The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes." Biochem J 1986;234(3);593-604. PMID: 3521591
Furumo95: Furumo NC, Kirsch JF (1995). "Accumulation of the quinonoid intermediate in the reaction catalyzed by aspartate aminotransferase with cysteine sulfinic acid." Arch Biochem Biophys 319(1);49-54. PMID: 7771805
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