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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 and aldehyde

Angeles TS, Viola RE. The kinetic mechanisms of the bifunctional enzyme aspartokinase-homoserine dehydrogenase I from Escherichia coli. Arch. Biochem. Biophys. 283: 96-101 (1990).

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

Baril C, Richaud C, Fournie E, Baranton G, Saint Girons I. Cloning of dapD, aroD and asd of Leptospira interrogans serovar icterohaemorrhagiae, and nucleotide sequence of the asd gene. J. Gen. Microbiol. 138: 47-53 (1992).

Biellmann JF, Eid P, Hirth C. Affinity labeling of the Escherichia coli aspartate-beta-semialdehyde dehydrogenase with an alkylating coenzyme analogue. Half-site reactivity and competition with the substrate alkylating analogue. Eur. J. Biochem. 104: 65-69 (1980).

Biellmann JF, Eid P, Hirth C, Jornvall H. Aspartate-beta-semialdehyde dehydrogenase from Escherichia coli. Purification and general properties. Eur. J. Biochem. 104: 53-58 (1980).

Biellmann JF, Eid P, Hirth C, Jornvall H. Aspartate-beta-semialdehyde dehydrogenase from Escherichia coli. Affinity labeling with the substrate analogue L-2-amino-4-oxo-5-chloropentanoic acid: an example of half-site reactivity. Eur. J. Biochem. 104: 59-64 (1980).

Blickling S, Renner C, Laber B, Pohlenz HD, Holak TA, Huber R. Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy. Biochemistry 36: 24-33 (1997).

Byun R, Elbourne LD, Lan R, Reeves PR. Evolutionary relationships of pathogenic clones of Vibrio cholerae by sequence analysis of four housekeeping genes. Infect. Immun. 67: 1116-1124 (1999).

Chassagnole C, Fell DA, Rais B, Kudla B, Mazat JP. Control of the threonine-synthesis pathway in Escherichia coli: a theoretical and experimental approach. Biochem. J. 356: 433-444 (2001).

Chen NY, Jiang SQ, Klein DA, Paulus H. Organization and nucleotide sequence of the Bacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase. J. Biol. Chem. 268: 9448-9465 (1993).

Cirillo JD, Weisbrod TR, Pascopella L, Bloom BR, Jacobs WR Jr. Isolation and characterization of the aspartokinase and aspartate semialdehyde dehydrogenase operon from mycobacteria. Mol. Microbiol. 11: 629-639 (1994).

Condon S, Collins JK, O'donovan GA. Regulation of arginine and pyrimidine biosynthesis in Pseudomonas putida. J. Gen. Microbiol. 92: 375-383 (1976).

Craciun A, Jacobs M, Vauterin M. Arabidopsis loss-of-function mutant in the lysine pathway points out complex regulation mechanisms. FEBS Lett. 487: 234-238 (2000).

Cremer J, Treptow C, Eggeling L, Sahm H. Regulation of enzymes of lysine biosynthesis in Corynebacterium glutamicum. J. Gen. Microbiol. 134: 3221-3229 (1988).

Eggeling L, Oberle S, Sahm H. Improved L-lysine yield with Corynebacterium glutamicum: use of dapA resulting in increased flux combined with growth limitation. Appl. Microbiol. Biotechnol. 49: 24-30 (1998).

Erecinska M, Nelson D, Daikhin Y, Yudkoff M. Regulation of GABA level in rat brain synaptosomes: fluxes through enzymes of the GABA shunt and effects of glutamate, calcium, and ketone bodies. J. Neurochem. 67: 2325-2334 (1996).

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).

Follettie MT, Peoples OP, Agoropoulou C, Sinskey AJ. Gene structure and expression of the Corynebacterium flavum N13 ask-asd operon. J. Bacteriol. 175: 4096-4103 (1993).

Fondi M, Brilli M, Fani R. On the origin and evolution of biosynthetic pathways: integrating microarray data with structure and organization of the Common Pathway genes. BMC Bioinformatics 8 Suppl. 1: S12 (2007).

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).

Hadfield A, Kryger G, Ouyang J, Petsko GA, Ringe D, Viola R. Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis. J. Mol. Biol. 289: 991-1002 (1999).

Hama H, Kayahara T, Tsuda M, Tsuchiya T. Inhibition of homoserine dehydrogenase I by L-serine in Escherichia coli. J. Biochem. (Tokyo) 109: 604-608 (1991).

Harb OS, Abu Kwaik Y. Identification of the aspartate-beta-semialdehyde dehydrogenase gene of Legionella pneumophila and characterization of a null mutant. Infect. Immun. 66: 1898-1903 (1998).

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).

Hoang TT, Schweizer HP. Identification and genetic characterization of the Pseudomonas aeruginosa leuB gene encoding 3-isopropylmalate dehydrogenase. Mol. Gen. Genet. 254: 166-170 (1997).

Hoang TT, Williams S, Schweizer HP, Lam JS. Molecular genetic analysis of the region containing the essential Pseudomonas aeruginosa asd gene encoding aspartate-beta-semialdehyde dehydrogenase. Microbiology 143: 899-907 (1997).

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).

Jagusztyn-Krynicka EK, Malaszewska-Keough A, Kauc B. Cloning and expression of Thiobacillus versutus aspartate-semialdehyde dehydrogenase gene in Escherichia coli. FEMS Microbiol. Lett. 50: 21-25 (1989).

Jagusztyn-Krynicka EK, Smorawinska M, Curtiss R 3d. Expression of Streptococcus mutans aspartate-semialdehyde dehydrogenase gene cloned into plasmid pBR322. J. Gen. Microbiol. 128: 1135-1145 (1982).

Jakobsen OM, Brautaset T, Degnes KF, Heggeset TM, Balzer S, Flickinger MC, Valla S, Ellingsen TE. Overexpression of wild-type aspartokinase increases L-lysine production in thermotolerant methylotrophic Bacillus methanolicus. Appl. Environ. Microbiol. 75: 652-661 (2009).

Jetten MS, Follettie MT, Sinskey AJ. Effect of different levels of aspartokinase on the lysine production by Corynebacterium lactofermentum. Appl. Microbiol. Biotechnol. 43: 76-82 (1995).

Kalinowski J, Bachmann B, Thierbach G, Puhler A. Aspartokinase genes lysC alpha and lysC beta overlap and are adjacent to the aspartate beta-semialdehyde dehydrogenase gene asd in Corynebacterium glutamicum. Mol. Gen. Genet. 224: 317-324 (1990).

Karsten WE. Dihydrodipicolinate synthase from Escherichia coli: pH dependent changes in the kinetic mechanism and kinetic mechanism of allosteric inhibition by L-lysine. Biochemistry 36: 1730-1739 (1997).

Karsten WE, Viola RE. Identification of an essential cysteine in the reaction catalyzed by aspartate-beta-semialdehyde dehydrogenase from Escherichia coli. Biochim. Biophys. Acta 1121: 234-238 (1992).

Karsten WE, Viola RE. Chemical and kinetic mechanisms of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli. Biochim. Biophys. Acta 1077: 209-219 (1991).

Kato C, Smorawinska M, Li L, Horikoshi K. Comparison of the gene expression of aspartate beta-D-semialdehyde dehydrogenase at elevated hydrostatic pressure in deep-sea bacteria. J. Biochem. (Tokyo) 121: 717-723 (1997).

Koo CW, Blanchard JS. Chemical mechanism of Haemophilus influenzae diaminopimelate epimerase. Biochemistry 38: 4416-4422 (1999).

Kryger G, Petsko GA, Ouyang J, Viola RE. Crystallization and preliminary crystallographic analysis of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli. J. Mol. Biol. 228: 300-301 (1992).

Laber B, Gomis-Ruth FX, Romao MJ, Huber R. Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization. Biochem. J. 288: 691-695 (1992).

Le Y, He J, Vining LC. Streptomyces akiyoshiensis differs from other gram-positive bacteria in the organization of a core biosynthetic pathway gene for aspartate family amino acids. Microbiology 142: 791-798 (1996).

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).

McKnight JA, Hird FJ. The oxidation of proline by mitochondrial preparations. Comp. Biochem. Physiol. [B.] 85: 289-294 (1986).

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).

Nosticzius A. Role of formaldehyde in direct formation of glycine and serine in bean leaves. Acta Biol. Hung. 49: 193-199 (1998).

Ouyang J, Viola RE. Use of structural comparisons to select mutagenic targets in aspartate-beta-semialdehyde dehydrogenase. Biochemistry 34: 6394-6399 (1995).

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

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).

Potrykus J, White RL, Bearne SL. Proteomic investigation of amino acid catabolism in the indigenous gut anaerobe Fusobacterium varium. Proteomics 8: 2691-2703 (2008).

Rais B, Mazat JP. Control of the metabolic pathway of threonine in E coli. Application of biotechnology. Acta Biotheor. 43: 143-153 (1995).

Rees WD, Hay SM. The biosynthesis of threonine by mammalian cells: expression of a complete bacterial biosynthetic pathway in an animal cell. Biochem. J. 309: 999-1007 (1995).

Romisch-Margl W, Schramek N, Radykewicz T, Ettenhuber C, Eylert E, Huber C, Romisch-Margl L, Schwarz C, Dobner M, Demmel N, Winzenhorlein B, Bacher A, Eisenreich W. (13)CO(2) as a universal metabolic tracer in isotopologue perturbation experiments. Phytochemistry 68: 2273-2289 (2007).

Sahm H, Eggeling L, Eikmanns B, Kramer R. Construction of L-lysine-, L-threonine-, and L-isoleucine-overproducing strains of Corynebacterium glutamicum. Ann. N.Y. Acad. Sci. 782: 25-39 (1996).

Sahm H, Eggeling L, Morbach S, Eikmanns B. Construction of L-isoleucine overproducing strains of Corynebacterium glutamicum. Naturwissenschaften 86: 33-38 (1999).

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).

Shames SL, Wedler FC. Homoserine kinase of Escherichia coli: kinetic mechanism and inhibition by L-aspartate semialdehyde. Arch. Biochem. Biophys. 235: 359-370 (1984).

Shaul O, Galili G. Concerted regulation of lysine and threonine synthesis in tobacco plants expressing bacterial feedback-insensitive aspartate kinase and dihydrodipicolinate synthase. Plant Mol. Biol. 23: 759-768 (1993).

Shaw JF, Funkhouser JD, Smith VA, Smith WG. Additional effects of monovalent cations on the lysine-sensitive aspartokinase of E. coli B. J. Inorg. Biochem. 18: 49-58 (1983).

Suzuki H, Ohnishi Y, Furusho Y, Sakuda S, Horinouchi S. Novel benzene ring biosynthesis from C3 and C4 primary metabolites by two enzymes. J. Biol. Chem. 281: 36944-36951 (2006).

Szczesiul M, Wampler DE. Regulation of a metabolic system in vitro: synthesis of threonine from aspartic acid. Biochemistry 15: 2236-2244 (1976).

Thierry JC, Moras D, Eid P, Hirth C. Crystallization of E. coli aspartate beta-semialdehyde dehydrogenase. Biochimie 62: 739-740 (1980).

Vauterin M, Frankard V, Jacobs M. The Arabidopsis thaliana dhdps gene encoding dihydrodipicolinate synthase, key enzyme of lysine biosynthesis, is expressed in a cell-specific manner. Plant Mol. Biol. 39: 695-708 (1999).

Vrljic M, Kronemeyer W, Sahm H, Eggeling L. Unbalance of L-lysine flux in Corynebacterium glutamicum and its use for the isolation of excretion-defective mutants. J. Bacteriol. 177: 4021-4027 (1995).

Wedler FC, Ley BW. Kinetic and regulatory mechanisms for (Escherichia coli) homoserine dehydrogenase-I. Equilibrium isotope exchange kinetics. J. Biol. Chem. 268: 4880-4888 (1993).

Wedler FC, Ley BW, Shames SL, Rembish SJ, Kushmaul DL. Preferred order random kinetic mechanism for homoserine dehydrogenase of Escherichia coli (Thr-sensitive) aspartokinase/homoserine dehydrogenase-I: equilibrium isotope exchange kinetics. Biochim. Biophys. Acta 1119: 247-249 (1992).

Yamaki H, Yamaguchi M, Tsuruo T, Yamaguchi H. Mechanism of action of an antifungal antibiotic, RI-331, (S) 2-amino-4-oxo-5-hydroxypentanoic acid; kinetics of inactivation of homoserine dehydrogenase from Saccharomyces cerevisiae. J. Antibiot. (Tokyo) 45: 750-755 (1992).

Zhang W, Jiang W, Zhao G, Yang Y, Chiao J. Sequence analysis and expression of the aspartokinase and aspartate semialdehyde dehydrogenase operon from rifamycin SV-producing Amycolatopsis mediterranei. Gene 237: 413-419 (1999).

Zhang WW, Jiang WH, Zhao GP, Yang YL, Chiao JS. Expression in Escherichia coli, purification and kinetic analysis of the aspartokinase and aspartate semialdehyde dehydrogenase from the rifamycin SV-producing Amycolatopsis mediterranei U32. Appl. Microbiol. Biotechnol. 54: 52-58 (2000).

Number of references = 70

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