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.
|Superclasses:||Degradation/Utilization/Assimilation → Amino Acids Degradation → Proteinogenic Amino Acids Degradation → L-aspartate Degradation|
In prokaryotes and eukaryotes the four-carbon amino acid aspartate is converted to the corresponding keto acid oxaloacetate by transamination using α-ketoglutarate as acceptor of the amino group. This reversible reaction also biosynthesizes aspartate (see pathway L-aspartate biosynthesis). Oxaloacetate is a tricarboxylic acid (TCA) cycle intermediate, as shown in the pathway link. Oxaloacetate can also be converted by phosphoenolpyruvate carboxykinase to phosphoenolpyruvate for use in gluconeogenesis (see pathway gluconeogenesis I). Aspartate is therefore a link between amino acid and carbohydrate metabolism. In addition, aspartate is a precursor for the biosynthesis of many other compounds including lysine, threonine, methionine and NAD+ (see aspartate superpathway and L-aspartate biosynthesis).
There are also several other routes for aspartate degradation. In mammals and most land vertebrates, aspartate can be degraded by entering the urea cycle at the point of citrulline, and is ultimately converted to fumarate (see pathway urea cycle). In another eukaryotic route, aspartate is degraded to malate as part of the reversible malate-aspartate shuttle found in liver, heart and kidney. This is one of several shuttle mechanisms used to transfer electrons from cytosolic NADH produced by glycolysis into the mitochondrion, because NADH itself cannot cross the inner mitochondrial membrane (see pathway L-aspartate degradation II). In prokaryotes, aspartate can be degraded to fumarate by aspartate ammonia-lyase (see pathway L-glutamate degradation II). [Voet04] [Gottschalk86] [Salway04b]
Variants: L-aspartate degradation II
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
Birolo91: Birolo L, Arnone MI, Cubellis MV, Andreotti G, Nitti G, Marino G, Sannia G (1991). "The active site of Sulfolobus solfataricus aspartate aminotransferase." Biochim Biophys Acta 1080(3);198-204. PMID: 1954227
Cronin91: Cronin VB, Maras B, Barra D, Doonan S (1991). "The amino acid sequence of the aspartate aminotransferase from baker's yeast (Saccharomyces cerevisiae)." Biochem J 277 ( Pt 2);335-40. PMID: 1859361
Cubellis89: Cubellis MV, Rozzo C, Nitti G, Arnone MI, Marino G, Sannia G (1989). "Cloning and sequencing of the gene coding for aspartate aminotransferase from the thermoacidophilic archaebacterium Sulfolobus solfataricus." Eur J Biochem 186(1-2);375-81. PMID: 2513189
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.
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
Horio88: Horio Y, Tanaka T, Taketoshi M, Nagashima F, Tanase S, Morino Y, Wada H (1988). "Rat cytosolic aspartate aminotransferase: molecular cloning of cDNA and expression in Escherichia coli." J Biochem (Tokyo) 103(5);797-804. PMID: 3053674
Leung81: Leung FY, Henderson AR (1981). "Isolation and purification of aspartate aminotransferase isoenzymes from human liver by chromatography and isoelectric focusing." Clin Chem 27(2);232-8. PMID: 7460273
Liu07a: Liu D, Pozharski E, Lepore BW, Fu M, Silverman RB, Petsko GA, Ringe D (2007). "Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals "a tale of two mechanisms"." Biochemistry 46(37);10517-27. PMID: 17713924
Marino88: Marino G, Nitti G, Arnone MI, Sannia G, Gambacorta A, De Rosa M (1988). "Purification and characterization of aspartate aminotransferase from the thermoacidophilic archaebacterium Sulfolobus solfataricus." J Biol Chem 263(25);12305-9. PMID: 3137225
Miyahara94: Miyahara I, Hirotsu K, Hayashi H, Kagamiyama H (1994). "X-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from Escherichia coli in three forms." J Biochem (Tokyo) 116(5);1001-12. PMID: 7896726
Muriana91: Muriana FJ, Alvarez-Ossorio MC, Relimpio AM (1991). "Purification and characterization of aspartate aminotransferase from the halophile archaebacterium Haloferax mediterranei." Biochem J 278 ( Pt 1);149-54. PMID: 1909112
Nagashima89: Nagashima F, Tanase S, Fukumoto Y, Joh T, Nomiyama H, Tsuzuki T, Shimada K, Kuramitsu S, Kagamiyama H, Morino Y (1989). "cDNA cloning and expression of pig cytosolic aspartate aminotransferase in Escherichia coli: amino-terminal heterogeneity of expressed products and lack of its correlation with enzyme function." Biochemistry 28(3);1153-60. PMID: 2653435
Numazawa89: Numazawa T, Yamada S, Hase T, Sugiyama T (1989). "Aspartate aminotransferase from Panicum maximum Jacq. var. trichoglume Eyles, a C4 plant: purification, molecular properties, and preparation of antibody." Arch Biochem Biophys 270(1);313-9. PMID: 2930193
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