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discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Pathway: aspartate degradation I

Enzyme View:

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 Aspartate Degradation

Some taxa known to possess this pathway include ? : Haloferax mediterranei , Pseudoalteromonas haloplanktis TAC125 , Rattus norvegicus , Saccharomyces cerevisiae , Sulfolobus solfataricus

Expected Taxonomic Range: Archaea , Bacteria , Eukaryota

Summary:
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 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 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 aspartate degradation II). In prokaryotes, aspartate can be degraded to fumarate by aspartate ammonia-lyase (see pathway glutamate degradation II). [Voet04] [Gottschalk86] [Salway04]

Variants: aspartate degradation II

Credits:
Revised 01-Mar-2007 by Fulcher CA , SRI International


References

Gottschalk86: Gottschalk, G "Bacterial Metabolism, Second Edition." Springer-Verlag, New York. 1986.

Salway04: Salway JG (2004). "Metabolism at a Glance." 3rd ed, Blackwell Publishing, Malden, MA, USA.

Voet04: Voet D, Voet JG (2004). "Biochemistry, 3rd Edition." John Wiley & Sons Inc.

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

Akagi82: Akagi R (1982). "Purification and characterization of cysteine aminotransferase from rat liver cytosol." Acta Med Okayama 36(3);187-97. PMID: 7113743

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

Han01: Han Q, Fang J, Li J (2001). "Kynurenine aminotransferase and glutamine transaminase K of Escherichia coli: identity with aspartate aminotransferase." Biochem J 360(Pt 3);617-23. PMID: 11736651

Helgadottir07: Helgadottir S, Rosas-Sandoval G, Soll D, Graham DE (2007). "Biosynthesis of phosphoserine in the Methanococcales." J Bacteriol 189(2);575-82. PMID: 17071763

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

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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

Liu07: 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

Michuda70: Michuda CM, Martinez-Carrion M (1970). "The isozymes of glutamate-aspartate transaminase. Mechanism of inhibition of dicarboxylic acids." J Biol Chem 245(2);262-9. PMID: 4312670

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

Morin92: Morin PJ, Subramanian GS, Gilmore TD (1992). "AAT1, a gene encoding a mitochondrial aspartate aminotransferase in Saccharomyces cerevisiae." Biochim Biophys Acta 1171(2);211-4. PMID: 1482685

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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Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Tue Nov 25, 2014, biocyc13.