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N Use By Plants
Nitrate Assimilation
Ammonia Assimilation
Glu, Gln, Asn, Gly, Ser
Aminotransferases
Asp, Ala, GABA
Val, Leu, Ileu, Thr, Lys
Pro, Arg, Orn
Polyamines
Non-protein AAs
Alkaloids
Sulfate Assimilation
Cys, Met, AdoMet, ACC
His, Phe, Tyr, Tryp
Secondary Products
Onium Compounds
Enzymes
Methods
Simulation
References
HORT640 - Metabolic Plant Physiology

References, aspartate aminotransferase

Abdelmalek MF, Angulo P, Jorgensen RA, Sylvestre PB, Lindor KD. Betaine, a promising new agent for patients with nonalcoholic steatohepatitis: results of a pilot study. Am. J. Gastroenterol. 96: 2711-2717 (2001).

Ahmad I, Hellebust JA. A spectrophotometric procedure for measuring oxoglutarate and determining aminotransferase activities using nicotinamide adenine dinucleotide phosphate-linked glutamate dehydrogenase from algae. Anal. Biochem. 180: 99-104 (1989).

Ajayi OB, Odutuga A. Effect of low-zinc status and essential fatty acids deficiency on the activities of aspartate aminotransferase and alanine aminotransferase in liver and serum of albino rats. Nahr. Food 48: 88-90 (2004).

Almo SC, Smith DL, Danishefsky AT, Ringe D. The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli. Protein Eng. 7: 405-412 (1994).

Arruda P, Kemper EL, Papes F, Leite A. Regulation of lysine catabolism in higher plants. Trends Plant Sci. 5: 324-330 (2000).

Azzariti A, Vacca RA, Giannattasio S, Merafina RS, Marra E, Doonan S. Kinetic properties and thermal stabilities of mutant forms of mitochondrial aspartate aminotransferase. Biochim. Biophys. Acta 1386: 29-38 (1998).

Bedell JP, Chalot M, Garnier A, Botton B. Effects of nitrogen source on growth and activity of nitrogen-assimilating enzymes in Douglas-fir seedlings. Tree Physiol. 19: 205-210 (1999).

Bibiano Melo JF, Lundstedt LM, Meton I, Baanante IV, Moraes G. Effects of dietary levels of protein on nitrogenous metabolism of Rhamdia quelen (Teleostei: Pimelodidae). Comp. Biochem. Physiol. A. Mol. Integr. Physiol. 145: 181-187 (2006).

Birolo L, Dal Piaz F, Pucci P, Marino G. Structural characterization of the M* partly folded intermediate of wild type and P138A aspartate aminotransferase from Escherichia coli. J. Biol. Chem. 277: 17428-17437 (2002).

Birolo L, Malashkevich VN, Capitani G, De Luca F, Moretta A, Jansonius JN, Marino G. Functional and structural analysis of cis-proline mutants of Escherichia coli aspartate aminotransferase. Biochemistry 38: 905-913 (1999).

Birolo L, Tutino ML, Fontanella B, Gerday C, Mainolfi K, Pascarella S, Sannia G, Vinci F, Marino G. Aspartate aminotransferase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125. Cloning, expression, properties, and molecular modelling. Eur. J. Biochem. 267: 2790-2802 (2000).

Bonarius HP, Houtman JH, de Gooijer CD, Tramper J, Schmid G. Activity of glutamate dehydrogenase is increased in ammonia-stressed hybridoma cells. Biotechnol. Bioeng. 57: 447-453 (1998).

Bonner CA, Fischer RS, Ahmad S, Jensen RA. Remnants of an ancient pathway to L-phenylalanine and L-tyrosine in enteric bacteria: evolutionary implications and biotechnological impact. Appl. Environ. Microbiol. 56: 3741-3747 (1990).

Bonner CA, Jensen RA. Novel features of prephenate aminotransferase from cell cultures of Nicotiana silvestris. Arch. Biochem. Biophys. 238: 237-246 (1985).

Bono H, Ogata H, Goto S, Kanehisa M. Reconstruction of amino acid biosynthesis pathways from the complete genome sequence. Genome Res. 8: 203-210 (1998).

Bradbury MW, Berk PD. Mitochondrial aspartate aminotransferase: direction of a single protein with two distinct functions to two subcellular sites does not require alternative splicing of the mRNA. Biochem. J. 345: 423-427 (2000).

Bray JE, Todd AE, Pearl FM, Thornton JM, Orengo CA. The CATH Dictionary of Homologous Superfamilies (DHS): a consensus approach for identifying distant structural homologues. Protein Eng. 13: 153-165 (2000).

Capitani G, Hohenester E, Feng L, Storici P, Kirsch JF, Jansonius JN. Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene. J. Mol. Biol. 294: 745-756 (1999).

Chatziioannou A, Palaiologos G, Kolisis FN. Metabolic flux analysis as a tool for the elucidation of the metabolism of neurotransmitter glutamate. Metab. Eng. 5: 201-210 (2003).

Chopra J, Kaur N, Gupta AK. The role of ammonium assimilating enzymes in lentil roots and nodules. Biol. Plant. 47: 105-109 (2003).

Chung YL, Rider LG, Bell JD, Summers RM, Zemel LS, Rennebohm RM, Passo MH, Hicks J, Miller FW, Scott DL; Juvenile Dermatomyositis Disease Activity Collaborative Study Group. Muscle metabolites, detected in urine by proton spectroscopy, correlate with disease damage in juvenile idiopathic inflammatory myopathies. Arthritis Rheum. 53: 565-570 (2005).

Collins N, Merrett MJ. The localization of glycollate-pathway enzymes in Euglena. Biochem. J. 148: 321-328 (1975).

Contador CA, Rizk ML, Asenjo JA, Liao JC. Ensemble modeling for strain development of L-lysine-producing Escherichia coli. Metab. Eng. 11: 221-233 (2009).

Contestabile R, John RA. The mechanism of high-yielding chiral syntheses catalysed by wild-type and mutant forms of aspartate aminotransferase. Eur. J. Biochem. 240: 150-155 (1996).

Cronin CN, Kirsch JF. Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis. Biochemistry 27: 4572-4579 (1988).

Danishefsky AT, Onnufer JJ, Petsko GA, Ringe D. Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase. Biochemistry 30: 1980-1985 (1991).

de la Torre F, De Santis L, Suarez MF, Crespillo R, Canovas FM. Identification and functional analysis of a prokaryotic-type aspartate aminotransferase: implications for plant amino acid metabolism. Plant J. 46: 414-425 (2006).

de la Torre F, Moya-Garcia AA, Suarez MF, Rodriguez-Caso C, Canas RA, Sanchez-Jimenez F, Canovas FM. Molecular modeling and site-directed mutagenesis reveal essential residues for catalysis in a prokaryote-type aspartate aminotransferase. Plant Physiol. 149: 1648-1660 (2009).

de la Torre F, Suarez MF, Santis L, Canovas FM. The aspartate aminotransferase family in conifers: biochemical analysis of a prokaryotic-type enzyme from maritime pine. Tree Physiol. 27: 1283-1291 (2007).

Deborde C, Rolin DB, Boyaval P. In vivo 13C NMR study of the bidirectional reactions of the Wood-Werkman cycle and around the pyruvate node in Propionibacterium freudenreichii subsp. shermanii and Propionibacterium acidipropionici. Metab. Eng. 1: 309-319 (1999).

Denessiouk KA, Denesyuk AI, Lehtonen JV, Korpela T, Johnson MS. Common structural elements in the architecture of the cofactor-binding domains in unrelated families of pyridoxal phosphate-dependent enzymes. Proteins 35: 250-261 (1999).

Dever LV, Blackwell RD, Fullwood NJ, Lacuesta M, Leegood RC, Onek LA, Pearson M, Lea PJ. The isolation and characterization of mutants of the C4 photosynthetic pathway. J. Exp. Bot. 46: 1363-1376 (1995).

Dolzan M, Johansson K, Roig-Zamboni V, Campanacci V, Tegoni M, Schneider G, Cambillau C. Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function. FEBS Lett. 571: 141-146 (2004).

Drsata J. Tryptophan metabolism via transamination. In vitro aminotransferase assay using dinitrophenylhydrazine method. Adv. Exp. Med. Biol. 527: 511-517 (2003).

Dry IB, Dimitriadis E, Ward AD, Wiskich JT. The photorespiratory hydrogen shuttle. Synthesis of phthalonic acid and its use in the characterization of the malate/aspartate shuttle in pea (Pisum sativum) leaf mitochondria. Biochem. J. 245: 669-675 (1987).

Eads JC, Beeby M, Scapin G, Yu TW, Floss HG. Crystal structure of 3-amino-5-hydroxybenzoic acid (AHBA) synthase. Biochemistry 38: 9840-9849 (1999).

Endo S, Ishiguro S, Tamai M. Possible mechanism for the decrease of mitochondrial aspartate aminotransferase activity in ischemic and hypoxic rat retinas. Biochim. Biophys. Acta 1450: 385-396 (1999).

Famiani F, Walker RP, Tecsi L, Chen ZH, Proietti P, Leegood RC. An immunohistochemical study of the compartmentation of metabolism during the development of grape (Vitis vinifera L.) berries. J. Exp. Bot. 51: 675-683 (2000).

Fitzgerald C, Swearengin TA, Yeargans G, McWhorter D, Cucchetti B, Seidler NW. Non-enzymatic glycosylation (or glycation) and inhibition of the pig heart cytosolic aspartate aminotransferase by glyceraldehyde 3-phosphate. J. Enzyme Inhib. 15: 79-89 (2000).

Gajewska E, Sklodowska M. Nickel-induced changes in nitrogen metabolism in wheat shoots. J. Plant Physiol. 166: 1034-1044 (2009).

Garrido-Franco M, Ehlert S, Messerschmidt A, Marinkovic S, Huber R, Laber B, Bourenkov GP, Clausen T. Structure and function of threonine synthase from yeast. J. Biol. Chem. 277: 12396-12405 (2002).

Gebhardt JS, Wadsworth GJ, Matthews BF. Characterization of a single soybean cDNA encoding cytosolic and glyoxysomal isozymes of aspartate aminotransferase. Plant Mol. Biol. 37: 99-108 (1998).

Geck MK, Kirsch JF. A novel, definitive test for substrate channeling illustrated with the aspartate aminotransferase/malate dehydrogenase system. Biochemistry 38: 8032-8037 (1999).

Gluck MR, Thomas RG, Davis KL, Haroutunian V. Implications for altered glutamate and GABA metabolism in the dorsolateral prefrontal cortex of aged schizophrenic patients. Am. J. Psychiat. 159: 1165-1173 (2002).

Gong J, Hunter GA, Ferreira GC. Aspartate-279 in aminolevulinate synthase affects enzyme catalysis through enhancing the function of the pyridoxal 5'-phosphate cofactor. Biochemistry 37: 3509-3517 (1998).

Graber R, Kasper P, Malashkevich VN, Sandmeier E, Berger P, Gehring H, Jansonius JN, Christen P. Changing the reaction specificity of a pyridoxal-5'-phosphate-dependent enzyme. Eur. J. Biochem. 232: 686-690 (1995).

Graber R, Kasper P, Malashkevich VN, Strop P, Gehring H, Jansonius JN, Christen P. Conversion of aspartate aminotransferase into an L-aspartate beta-decarboxylase by a triple active-site mutation. J. Biol. Chem. 274: 31203-31208 (1999).

Gregerson RG, Miller SS, Petrowski M, Gantt JS, Vance CP. Genomic structure, expression and evolution of the alfalfa aspartate aminotransferase genes. Plant Mol. Biol. 25: 387-399 (1994).

Gregerson RG, Petrowski M, Larson RL, Gantt JS, Vance CP. Molecular analysis of allelic polymorphism at the AAT2 locus of alfalfa. Mol. Gen. Genet. 241: 124-128 (1993).

Hagishita T, Yoshida T, Izumi Y, Mitsunaga T. Cloning and expression of the gene for serine-glyoxylate aminotransferase from an obligate methylotroph Hyphomicrobium methylovorum GM2. Eur. J. Biochem. 241: 1-5 (1996).

Hasegawa T, Mihara M, Nakamuro K, Sayato Y. Mechanisms of selenium methylation and toxicity in mice treated with selenocystine. Arch. Toxicol. 71: 31-38 (1996).

Hassel B, Boldingh KA, Narvesen C, Iversen EG, Skrede KK. Glutamate transport, glutamine synthetase and phosphate-activated glutaminase in rat CNS white matter. A quantitative study. J. Neurochem. 87: 230-237 (2003).

Hennig M, Grimm B, Contestabile R, John RA, Jansonius JN. Crystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity. Proc. Natl. Acad. Sci. U.S.A. 94: 4866-4871 (1997).

Hester G, Stark W, Moser M, Kallen J, Markovic-Housley Z, Jansonius JN. Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 A resolution: comparison of the unligated enzyme and a complex with alpha-methyl-L-glutamate. J. Mol. Biol. 286: 829-850 (1999).

Hodges M. Enzyme redundancy and the importance of 2-oxoglutarate in plant ammonium assimilation. J. Exp. Bot. 53: 905-916 (2002).

Hoedemaeker FJ, Davidson AR, Rose DR. A model for the nucleotide-binding domains of ABC transporters based on the large domain of aspartate aminotransferase. Proteins 30: 275-286 (1998).

Huang H, Yu Y, Yi X, Zhang Y. Nitrogen metabolism of asparagine and glutamate in Vero cells studied by (1)H/ (15)N NMR spectroscopy. Appl. Microbiol. Biotechnol. 77: 427-436 (2007).

Inokuchi R, Kuma KI, Miyata T, Okada M. Nitrogen-assimilating enzymes in land plants and algae: phylogenic and physiological perspectives. Physiol. Plant. 116: 1 (2002).

Inoue K, Kuramitsu S, Aki K, Watanabe Y, Takagi T, Nishigai M, Ikai A, Kagamiyama H. Branched-chain amino acid aminotransferase of Escherichia coli: overproduction and properties. J. Biochem. (Tokyo) 104: 777-784 (1988).

Inoue K, Kuramitsu S, Okamoto A, Hirotsu K, Higuchi T, Morino Y, Kagamiyama H. Tyr225 in aspartate aminotransferase: contribution of the hydrogen bond between Tyr225 and coenzyme to the catalytic reaction. J. Biochem. (Tokyo) 109: 570-576 (1991).

Ishijima J, Nakai T, Kawaguchi S, Hirotsu K, Kuramitsu S. Free energy requirement for domain movement of an enzyme. J. Biol. Chem. 275: 18939-18945 (2000).

Isupov MN, Antson AA, Dodson EJ, Dodson GG, Dementieva IS, Zakomirdina LN, Wilson KS, Dauter Z, Lebedev AA, Harutyunyan EH. Crystal structure of tryptophanase. J. Mol. Biol. 276: 603-623 (1998).

Jacob C, Anwar A, Burkholz T. Perspective on recent developments on sulfur-containing agents and hydrogen sulfide signaling. Planta Med. 74: 1580-1592 (2008).

Jadaho SB, Yang RZ, Lin Q, Hu H, Anania FA, Shuldiner AR, Gong DW. Murine alanine aminotransferase: cDNA cloning, functional expression, and differential gene regulation in mouse fatty liver. Hepatology 39: 1297-1302 (2004).

Jeffery CJ, Barry T, Doonan S, Petsko GA, Ringe D. Crystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase. Protein Sci. 7: 1380-1387 (1998).

Jeffery CJ, M Gloss L, A Petsko G, Ringe D. The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase. Protein Eng. 13: 105-112 (2000).

Jhee KH, Yang LH, Ahmed SA, McPhie P, Rowlett R, Miles EW. Mutation of an active site residue of tryptophan synthase (beta-serine 377) alters cofactor chemistry. J. Biol. Chem. 273: 11417-11422 (1998).

Kim YC, Jung YS, Kim SK. Effect of betaine supplementation on changes in hepatic metabolism of sulfur-containing amino acids and experimental cholestasis induced by alpha-naphthylisothiocyanate. Food Chem. Toxicol. 43: 663-670 (2005).

Kirk CA, Mett V, Reynolds PH. The aspartate aminotransferase-P1 gene from Lupinus angustifolius. Plant Physiol. 105: 763-764 (1994).

Ko TP, Wu SP, Yang WZ, Tsai H, Yuan HS. Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase. Acta Crystallogr. D. Biol. Crystallogr. 55: 1474-1477 (1999).

Kondo K, Wakabayashi S, Kagamiyama H. Structural studies on aspartate aminotransferase from Escherichia coli. Covalent structure. J. Biol. Chem. 262: 8648-8657 (1987).

Kondo K, Wakabayashi S, Yagi T, Kagamiyama H. The complete amino acid sequence of aspartate aminotransferase from Escherichia coli: sequence comparison with pig isoenzymes. Biochem. Biophys. Res. Commun. 122: 62-67 (1984).

Kugler P. Enzymes involved in glutamatergic and GABAergic neurotransmission. Int. Rev. Cytol. 147: 285-336 (1993).

Kumar N, Kumar S, Vats SK, Ahuja PS. Effect of altitude on the primary products of photosynthesis and the associated enzymes in barley and wheat. Photosynth. Res. 88: 63-71 (2006).

Kuramitsu S, Inoue K, Ogawa T, Ogawa H, Kagamiyama H. Aromatic amino acid aminotransferase of Escherichia coli: nucleotide sequence of the tyrB gene. Biochem. Biophys. Res. Commun. 133: 134-139 (1985).

Kuramitsu S, Okuno S, Ogawa T, Ogawa H, Kagamiyama H. Aspartate aminotransferase of Escherichia coli: nucleotide sequence of the aspC gene. J. Biochem. (Tokyo) 97: 1259-1262 (1985).

Kwok EY, Hanson MR. GFP-labelled Rubisco and aspartate aminotransferase are present in plastid stromules and traffic between plastids. J. Exp. Bot. 55: 595-604 (2004).

Lain B, Yanez A, Iriarte A, Martinez-Carrion M. Aminotransferase variants as probes for the role of the N-terminal region of a mature protein in mitochondrial precursor import and processing. J. Biol. Chem. 273: 4406-4415 (1998).

Lam HM, Coschigano KT, Oliveira IC, Melo-Oliveira R, Coruzzi GM. The molecular-genetics of nitrogen assimilation into amino acids in higher plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 47: 569-593 (1996).

Lawton JM, Doonan S. Thermal inactivation and chaperonin-mediated renaturation of mitochondrial aspartate aminotransferase. Biochem. J. 334: 219-224 (1998).

Le Roux MR, Khan S, Valentine AJ. Organic acid accumulation may inhibit N2 fixation in phosphorus-stressed lupin nodules. New Phytol. 177: 956-964 (2008).

Ledwidge R, Blanchard JS. The dual biosynthetic capability of N-acetylornithine aminotransferase in arginine and lysine biosynthesis. Biochemistry 38: 3019-3024 (1999).

Lee J, Sperandio V, Frantz DE, Longgood J, Camilli A, Phillips MA, Michael AJ. An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae. J. Biol. Chem. 284: 9899-9907 (2009).

Liang Z, Yu C, Huang AH. Conversion of glycerate to serine in intact spinach leaf peroxisomes. Arch. Biochem. Biophys. 233: 393-401 (1984).

Liepman AH, Olsen LI. Genomic analysis of aminotransferases in Arabidopsis thaliana. Crit. Rev. Plant Sci. 23: 73-89 (2004).

Mahon MM, Graber R, Christen P, Malthouse JP. The aspartate aminotransferase-catalysed exchange of the alpha-protons of aspartate and glutamate: the effects of the R386A and R292V mutations on this exchange reaction. Biochim. Biophys. Acta 1434: 191-201 (1999).

Malashkevich VN, Jager J, Ziak M, Sauder U, Gehring H, Christen P, Jansonius JN. Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue. Biochemistry 34: 405-414 (1995).

Malthankar-Phatak GH, de Lanerolle N, Eid T, Spencer DD, Behar KL, Spencer SS, Kim JH, Lai JC. Differential glutamate dehydrogenase (GDH) activity profile in patients with temporal lobe epilepsy. Epilepsia 47: 1292-1299 (2006).

Marchenko GN, Marchenko ND, Tsygankov YD, Chistoserdov AY. Organization of threonine biosynthesis genes from the obligate methylotroph Methylobacillus flagellatus. Microbiology 145: 3273-3282 (1999).

Mehta PK, Christen P. Homology of 1-aminocyclopropane-1-carboxylate synthase, 8-amino-7-oxononanoate synthase, 2-amino-6-caprolactam racemase, 2,2-dialkylglycine decarboxylase, glutamate-1-semialdehyde 2,1-aminomutase ... with aminotransferases. Biochem. Biophys. Res. Commun. 198: 138-143 (1994).

Mehta PK, Christen P. The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes. Adv. Enzymol. Relat. Areas Mol. Biol. 74: 129-184 (2000).

Mehta PK, Hale TI, Christen P. Evolutionary relationships among aminotransferases. Tyrosine aminotransferase, histidinol-phosphate aminotransferase, and aspartate aminotransferase are homologous proteins. Eur. J. Biochem. 186: 249-253 (1989).

Mehta PK, Hale TI, Christen P. Aminotransferases: demonstration of homology and division into evolutionary subgroups. Eur. J. Biochem. 214: 549-561 (1993).

Meister M, Agostino A, Hatch MD. The roles of malate and aspartate in C4 photosynthetic metabolism of Flaveria bidentis (L). Planta 199: 262-269 (1996).

Mett V, Mett VL, Reynolds PH. The aspartate aminotransferase-P2 gene from Lupinus angustifolius. Plant Physiol. 106: 1683-1684 (1994).

Miesak BH, Coruzzi GM. Molecular and physiological analysis of Arabidopsis mutants defective in cytosolic or chloroplastic aspartate aminotransferase. Plant Physiol. 129: 650-660 (2002).

Moran J, Alavez S, Rivera-Gaxiola M, Valencia A, Hurtado S. Effect of NMDA antagonists on the activity of glutaminase and aspartate aminotransferase in the developing rat cerebellum. Int. J. Dev. Neurosci. 17: 57-65 (1999).

Morgunov I, Srere PA. Interaction between citrate synthase and malate dehydrogenase. Substrate channeling of oxaloacetate. J. Biol. Chem. 273: 29540-29544 (1998).

Mouratou B, Kasper P, Gehring H, Christen P. Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature. J. Biol. Chem. 274: 1320-1325 (1999).

Muench DG, Archibold OW, Good AG. Hypoxic metabolism in wild rice (Zizania-palustris): enzyme-induction and metabolite production. Physiol. Plant. 89: 165-171 (1993).

Muscolo A, Panuccio MR, Sidari M, Sessi E, Nardi S. Alteration of amino acid metabolism by humic substances during germination of Pinus laricio seeds. Seed Sci. Technol. 30: 205-210 (2002).

Nakabachi A, Ishikawa H. Differential display of mRNAs related to amino acid metabolism in the endosymbiotic system of aphids. Insect Biochem. Mol. Biol. 27: 1057-1062 (1997).

Nakai T, Okada K, Akutsu S, Miyahara I, Kawaguchi S, Kato R, Kuramitsu S, Hirotsu K. Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate. Biochemistry 38: 2413-2424 (1999).

Nakai T, Okada K, Kawaguchi Si, Kato R, Kuramitsu S, Hirotsu K. Crystallization and preliminary X-ray characterization of aspartate aminotransferase from an extreme thermophile, Thermus thermophilus HB8. Acta Crystallogr. D. Biol. Crystallogr. 54: 1032-1034 (1998).

Neuffer B, Hurka H. Colonization history and introduction dynamics of Capsella bursa-pastoris (Brassicaceae) in North America: isozymes and quantitative traits. Mol. Ecol. 8: 1667-1681 (1999).

Newsholme P, Brennan L, Bender K. Amino acid metabolism, {beta}-cell function, and diabetes. Diabetes 55 Suppl. 2: S39-S47 (2006).

Obungu VH, Kiaira JK, Njogu RM, Olembo NK. Catabolism of proline by procyclic culture forms of Trypanosoma congolense. Comp. Biochem. Physiol. [B] 123: 59-65 (1999).

Okamoto A, Nakai Y, Hayashi H, Hirotsu K, Kagamiyama H. Crystal structures of Paracoccus denitrificans aromatic amino acid aminotransferase: a substrate recognition site constructed by rearrangement of hydrogen bond network. J. Mol. Biol. 280: 443-461 (1998).

Oue S, Okamoto A, Yano T, Kagamiyama H. Cocrystallization of a mutant aspartate aminotransferase with a C5-dicarboxylic substrate analog: structural comparison with the enzyme-C4-dicarboxylic analog complex. J. Biochem. (Tokyo) 127: 337-343 (2000).

Ovadi J, Srere PA. Macromolecular compartmentation and channeling. Int. Rev. Cytol. 192: 255-280 (2000).

Pandey R, Agarwal RM, Jeevaratnam K, Sharma GL. Osmotic stress-induced alterations in rice (Oryza sativa L.) and recovery on stress release. Plant Growth Regul. 42: 79-87 (2004).

Park LC, Gibson GE, Bunik V, Cooper AJ. Inhibition of select mitochondrial enzymes in PC12 cells exposed to S-(1,1,2,2-tetrafluoroethyl)-L-cysteine. Biochem. Pharmacol. 58: 1557-1565 (1999).

Pascarella S, Schirch V, Bossa F. Similarity between serine hydroxymethyltransferase and other pyridoxal phosphate-dependent enzymes. FEBS Lett. 331: 145-149 (1993).

Pascarella S, Schirch V, Bossa F. Similarity between serine hydroxymethyltransferase and other pyridoxal phosphate-dependent enzymes. FEBS Lett. 331: 145-149 (1993).

Paszkowski A, Niedzielska A. Glutamate:glyoxylate aminotransferase from the seedlings of rye (Secale cereale L.). Acta Biochim. Pol. 36: 17-29 (1989).

Petersen S, Mack C, De Graaf AA, Riedel C, Eikmanns BJ, Sahm H. Metabolic consequences of altered phosphoenolpyruvate carboxykinase activity in Corynebacterium glutamicum reveal anaplerotic regulation mechanisms in vivo. Metab. Eng. 3: 344-361 (2001).

Polakof S, Ceinos RM, Fernandez-Duran B, Miguez JM, Soengas JL. Daily changes in parameters of energy metabolism in brain of rainbow trout: dependence on feeding. Comp. Biochem. Physiol. A. Mol. Integr. Physiol. 146: 265-273 (2007).

Powell JT, Morrison JF. The purification and properties of the aspartate aminotransferase and aromatic-amino-acid aminotransferase from Escherichia coli. Eur. J. Biochem. 87: 391-400 (1978).

Qu K, Martin DL, Lawrence CE. Motifs and structural fold of the cofactor binding site of human glutamate decarboxylase. Protein Sci. 7: 1092-1105 (1998).

Quintero MJ, Muro-Pastor AM, Herrero A, Flores E. Arginine catabolism in the cyanobacterium Synechocystis sp. strain PCC 6803 involves the urea cycle and arginase pathway. J. Bacteriol. 182: 1008-1015 (2000).

Reed RE, Hess JL. Partial purification and characterization of aspartate aminotransferases from seedling oat leaves. J. Biol. Chem. 250: 4456-4461 (1975).

Rishavy MA, Cleland WW. 13C and 15N kinetic isotope effects on the reaction of aspartate aminotransferase and the tyrosine-225 to phenylalanine mutant. Biochemistry 39: 7546-7551 (2000).

Ro HS. Effects of salts on the conformation and catalytic properties of D-amino acid aminotransferase. J. Biochem. Mol. Biol. 35: 306-312 (2002).

Rosenthal GA, Dahlman DL. Interaction of L-canaline with ornithine aminotransferase of the tobacco hornworm, Manduca sexta (Sphingidae). J. Biol. Chem. 265: 868-873 (1990).

Rowsell EV, Carnie JA, Wahbi SD, Al-Tai AH, Rowsell KV. L-Serine dehydratase and L-serine-pyruvate aminotransferase activities in different animal species. Comp. Biochem. Physiol. [B] 63: 543-555 (1979).

Scapin G, Blanchard JS. Enzymology of bacterial lysine biosynthesis. Adv. Enzymol. Relat. Areas Mol. Biol. 72: 279-324 (1998).

Scarsdale JN, Radaev S, Kazanina G, Schirch V, Wright HT. Crystal structure at 2.4 A resolution of E. coli serine hydroxymethyltransferase in complex with glycine substrate and 5-formyl tetrahydrofolate. J. Mol. Biol. 296: 155-168 (2000).

Schiavon M, Ertani A, Nardi S. Effects of an alfalfa protein hydrolysate on the gene expression and activity of enzymes of the tricarboxylic acid (TCA) cycle and nitrogen metabolism in Zea mays L. J. Agric. Food Chem. 56: 11800-11808 (2008).

Schmid D, Jaussi R, Christen P. Precursor of mitochondrial aspartate aminotransferase synthesized in Escherichia coli is complexed with heat-shock protein DnaK. Eur. J. Biochem. 208: 699-704 (1992).

Schneider G, Kack H, Lindqvist Y. The manifold of vitamin B6 dependent enzymes. Structure Fold. Des. 8: R1-R6 (2000).

Schultz CJ, Coruzzi GM. The aspartate aminotransferase gene family of Arabidopsis encodes isoenzymes localized to three distinct subcellular compartments. Plant J. 7: 61-75 (1995).

Schultz CJ, Hsu M, Miesak B, Coruzzi GM. Arabidopsis mutants define an in vivo role for isoenzymes of aspartate aminotransferase in plant nitrogen assimilation. Genetics 149: 491-499 (1998).

Seebauer JR, Moose SP, Fabbri BJ, Crossland LD, Below FE. Amino acid metabolism in maize earshoots. Implications for assimilate preconditioning and nitrogen signaling. Plant Physiol. 136: 4326-4334 (2004).

Sentoku N, Taniguchi M, Sugiyama T, Ishimaru K, Ohsugi R, Takaiwa F, Toki S. Analysis of the transgenic tobacco plants expressing Panicum miliaceum aspartate aminotransferase genes. Plant Cell Rep. 19: 598-603 (2000).

Sherwin AL. Neuroactive amino acids in focally epileptic human brain: a review. Neurochem. Res. 24: 1387-1395 (1999).

Siehl DL, Connelly JA, Conn EE. Tyrosine biosynthesis in Sorghum bicolor: characteristics of prephenate aminotransferase. Z. Naturforsch. [C] 41: 79-86 (1986).

Silvente S, Camas A, Lara M. Molecular cloning of the cDNA encoding aspartate aminotransferase from bean root nodules and determination of its role in nodule nitrogen metabolism. J. Exp. Bot. 54: 1545-1551 (2003).

Takahashi N, Yamada T. Pathways for amino acid metabolism by Prevotella intermedia and Prevotella nigrescens. Oral Microbiol. Immunol. 15: 96-102 (2000).

Talwar R, Leelavathy V, Krishna Rao JV, Appaji Rao N, Savithri HS. Role of pro-297 in the catalytic mechanism of sheep liver serine hydroxymethyltransferase. Biochem. J. 350: 849-853 (2000).

Talwar R, Rao NA, Savithri HS. A change in reaction specificity of sheep liver serine hydroxymethyltransferase. Induction of NADH oxidation upon mutation of His230 to Tyr. Eur. J. Biochem. 267: 929-934 (2000).

Taniguchi M, Kobe A, Kato M, Sugiyama T. Aspartate aminotransferase isozymes in Panicum miliaceum L., an NAD-malic enzyme-type C4 plant: comparison of enzymatic properties primary structures, and expression patterns. Arch. Biochem. Biophys. 318: 295-306 (1995).

Taniguchi M, Sawaki H, Sasakawa H, Hase T, Sugiyama T. Cloning and sequence analysis of cDNA encoding aspartate aminotransferase isozymes from Panicum miliaceum L., a C4 plant. Eur. J. Biochem. 204: 611-620 (1992).

Tarun AS, Theologis A. Complementation analysis of mutants of 1-aminocyclopropane- 1-carboxylate synthase reveals the enzyme is a dimer with shared active sites. J. Biol. Chem. 273: 12509-12514 (1998).

Temple SJ, Vance CP, Gantt JS. Glutamate synthase and nitrogen assimilation. Trends Plant Sci. 3: 51-56 (1998).

Tharakan J, Hossenbocus A, Arthur MJ. Macromolecular aspartate aminotransferase. Eur. J. Gastroenterol. Hepatol. 10: 1055-1056 (1998).

Turano FJ, Weisemann JM, Matthews BF. Identification and expression of a cDNA clone encoding aspartate aminotransferase in carrot. Plant Physiol. 100: 374-381 (1992).

Uno S, Kaito M, Kobayashi Y, Ishida S, Kato H, Gabazza E, Tamaki S, Ikoma J, Imoto I, Watanabe S, Adachi Y. Case report: Alanine aminotransferase deficiency detected in a patient with chronic hepatitis C. J. Gastroenterol. Hepatol. 13: 480-482 (1998).

Vacca RA, Christen P, Malashkevich VN, Jansonius JN, Sandmeier E. Substitution of apolar residues in the active site of aspartate aminotransferase by histidine. Effects on reaction and substrate specificity. Eur. J. Biochem. 227: 481-487 (1995).

Vacca RA, Giannattasio S, Graber R, Sandmeier E, Marra E, Christen P. Active-site Arg --> Lys substitutions alter reaction and substrate specificity of aspartate aminotransferase. J. Biol. Chem. 272: 21932-21937 (1997).

Verleur N, Elgersma Y, Van Roermund CW, Tabak HF, Wanders RJ. Cytosolic aspartate aminotransferase encoded by the AAT2 gene is targeted to the peroxisomes in oleate-grown Saccharomyces cerevisiae. Eur. J. Biochem. 247: 972-980 (1997).

Villanueva JA, Halsted CH. Hepatic transmethylation reactions in micropigs with alcoholic liver disease. Hepatology 39: 1303-1310 (2004).

Vozarova B, Stefan N, Lindsay RS, Saremi A, Pratley RE, Bogardus C, Tataranni PA. High alanine aminotransferase is associated with decreased hepatic insulin sensitivity and predicts the development of type 2 diabetes. Diabetes 51: 1889-1895 (2002).

Wadsworth GJ, Gebhardt JS, Matthews BF. Characterization of a soybean cDNA clone encoding the mitochondrial isozyme of aspartate aminotransferase, AAT4. Plant Mol. Biol. 27: 1085-1095 (1995).

Walker RP, Chen ZH, Tecsi LI, Famiani F, Lea PJ, Leegood RC. Phosphoenolpyruvate carboxykinase plays a role in interactions of carbon and nitrogen metabolism during grape seed development. Planta 210: 9-18 (1999).

Watanabe N, Cherney MM, van Belkum MJ, Marcus SL, Flegel MD, Clay MD, Deyholos MK, Vederas JC, James MN. Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana: a recently discovered enzyme in the biosynthesis of L-lysine by plants and Chlamydia. J. Mol. Biol. 371: 685-702 (2007).

White MF, Vasquez J, Yang SF, Kirsch JF. Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization of wild-type and active-site mutant forms. Proc. Natl. Acad. Sci. U.S.A. 91: 12428-12432 (1994).

Widmann M, Christen P. Comparison of folding rates of homologous prokaryotic and eukaryotic proteins. J. Biol. Chem. 275: 18619-18622 (2000).

Wilkie MP, Claude JF, Cockshutt A, Holmes JA, Wang YS, Youson JH, Walsh PJ. Shifting patterns of nitrogen excretion and amino acid catabolism capacity during the life cycle of the sea lamprey (Petromyzon marinus). Physiol. Biochem. Zool. 79: 885-898 (2006).

Wilkie SE, Roper JM, Smith AG, Warren MJ. Isolation, characterisation and expression of a cDNA clone encoding plastid aspartate aminotransferase from Arabidopsis thaliana. Plant Mol. Biol. 27: 1227-1233 (1995).

Wilkie SE, Warren MJ. Recombinant expression, purification, and characterization of three isoenzymes of aspartate aminotransferase from Arabidopsis thaliana. Protein Expr. Purif. 12: 381-389 (1998).

Winefield CS, Farnden KJ, Reynolds PH, Marshall CJ. Evolutionary analysis of aspartate aminotransferases. J. Mol. Evol. 40: 455-463 (1995).

Winefield CS, Reddington BD, Jones WT, Reynolds PH, Farnden KJ. Cloning and characterization of a cDNA encoding aspartate aminotransferase-P1 from Lupinus angustifolius root tips. Plant Physiol. 104: 417-423 (1994).

Winiarska K, Bozko P, Lietz T, Bryla J. Importance of glutamate dehydrogenase stimulation for glucose and glutamine synthesis in rabbit renal tubules incubated with various amino acids. Acta Biochim. Pol. 45: 825-831 (1998).

Yano T, Oue S, Kagamiyama H. Directed evolution of an aspartate aminotransferase with new substrate specificities. Proc. Natl. Acad. Sci. U.S.A. 95: 5511-5515 (1998).

Yu C, Huang AH. Conversion of serine to glycerate in intact spinach leaf peroxisomes: role of malate dehydrogenase. Arch. Biochem. Biophys. 245: 125-133 (1986).

Yudkoff M, Daikhin Y, Nissim I, Nissim I. Acidosis and astrocyte amino acid metabolism. Neurochem. Int. 36: 329-339 (2000).

Zhebentiaeva TN. The polymorphism and inheritance of aspartate aminotransferase in apricot. Tsitol. Genet. 34: 57-62 (2000).

Number of references = 167

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