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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, adenylyl

Abell LM, Villafranca JJ. Effect of metal ions and adenylylation state on the internal thermodynamics of phosphoryl transfer in the Escherichia coli glutamine synthetase reaction. Biochemistry 30: 1413-1418 (1991).

Adler SP, Purich D, Stadtman ER. Cascade control of Escherichia coli glutamine synthetase. Properties of the PII regulatory protein and the uridylyltransferase-uridylyl-removing enzyme. J. Biol. Chem. 250: 6264-6272 (1975).

Aghajanian S, Worrall DM. Identification and characterization of the gene encoding the human phosphopantetheine adenylyltransferase and dephospho-CoA kinase bifunctional enzyme (CoA synthase). Biochem. J. 365: 13-18 (2002).

Allen JW, Shachar-Hill Y. Sulfur transfer through an arbuscular mycorrhiza. Plant Physiol. 149: 549-560 (2009).

Amon J, Titgemeyer F, Burkovski A. A genomic view on nitrogen metabolism and nitrogen control in mycobacteria. J. Mol. Microbiol. Biotechnol. 17: 20-29 (2009).

Antonyuk LP, Smirnova VE, Kamnev AA, Serebrennikova OB, Vanoni MA, Zanetti G, Kudelina IA, Sokolov OI, Ignatov VV. Influence of divalent cations on the catalytic properties and secondary structure of unadenylylated glutamine synthetase from Azospirillum brasilense. Biometals 14: 13-22 (2001).

Arcondeguy T, Huez I, Tillard P, Gangneux C, de Billy F, Gojon A, Truchet G, Kahn D. The Rhizobium meliloti PII protein, which controls bacterial nitrogen metabolism, affects alfalfa nodule development. Genes Dev. 11: 1194-1206 (1997).

Armengaud J, Fernandez B, Chaumont V, Rollin-Genetet F, Finet S, Marchetti C, Myllykallio H, Vidaud C, Pellequer JL, Gribaldo S, Forterre P, Gans P. Identification, purification, and characterization of an eukaryotic-like phosphopantetheine adenylyltransferase (coenzyme A biosynthetic pathway) in the hyperthermophilic archaeon Pyrococcus abyssi. J. Biol. Chem. 278: 31078-31087 (2003).

Atkins WM. Supramolecular self-assembly of Escherichia coli glutamine synthetase: effects of pressure and adenylylation state on dodecamer stacking. Biochemistry 33: 14965-14973 (1994).

Atkins WM, Cader BM, Hemmingsen J, Villafranca JJ. Time-resolved fluorescence and computational studies of adenylylated glutamine synthetase: analysis of intersubunit interactions. Protein Sci. 2: 800-813 (1993).

Atkins WM, Villafranca JJ. Time-resolved fluorescence studies of tryptophan mutants of Escherichia coli glutamine synthetase: conformational analysis of intermediates and transition-state complexes. Protein Sci. 1: 342-355 (1992).

Atkinson MR, Ninfa AJ. Role of the GlnK signal transduction protein in the regulation of nitrogen assimilation in Escherichia coli. Mol. Microbiol. 29: 431-447 (1998).

Atkinson MR, Ninfa AJ. Characterization of the GlnK protein of Escherichia coli. Mol. Microbiol. 32: 301-313 (1999).

Bancroft S, Rhee SG, Neumann C, Kustu S. Mutations that alter the covalent modification of glutamine synthetase in Salmonella typhimurium. J. Bacteriol. 134: 1046-1055 (1978).

Bascaran V, Hardisson C, Brana AF. Regulation of nitrogen catabolic enzymes in Streptomyces clavuligerus. J. Gen. Microbiol. 135: 2465-2474 (1989).

Berberich MA. Effect of some D-amino acids on the steady-state level of glutamine synthetase in Escherichia coli. J. Bacteriol. 163: 1109-1113 (1985).

Berendt U, Haverkamp T, Prior A, Schwenn JD. Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis. Eur. J. Biochem. 233: 347-356 (1995).

Berlett BS, Friguet B, Yim MB, Chock PB, Stadtman ER. Peroxynitrite-mediated nitration of tyrosine residues in Escherichia coli glutamine synthetase mimics adenylylation: relevance to signal transduction. Proc. Natl. Acad. Sci. U.S.A. 93: 1776-1780 (1996).

Berlett BS, Levine RL, Stadtman ER. Carbon dioxide stimulates peroxynitrite-mediated nitration of tyrosine residues and inhibits oxidation of methionine residues of glutamine synthetase: both modifications mimic effects of adenylylation. Proc. Natl. Acad. Sci. U.S.A. 95: 2784-2789 (1998).

Bevers LE, Hagedoorn PL, Santamaria-Araujo JA, Magalon A, Hagen WR, Schwarz G. Function of MoaB proteins in the biosynthesis of the molybdenum and tungsten cofactors. Biochemistry 47: 949-956 (2008).

Bibart RT, Vogel KW, Drueckhammer DG. Development of a second generation Coenzyme A analogue synthon. J. Org. Chem. 64: 2903-2909 (1999).

Bick JA, Aslund F, Chen Y, Leustek T. Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5'-adenylylsulfate reductase. Proc. Natl. Acad. Sci. U.S.A. 95: 8404-8409 (1998).

Bick JA, Dennis JJ, Zylstra GJ, Nowack J, Leustek T. Identification of a new class of 5'-adenylylsulfate (APS) reductases from sulfate-assimilating bacteria. J. Bacteriol. 182: 135-142 (2000).

Bick JA, Leustek T. Plant sulfur metabolism - the reduction of sulfate to sulfite. Curr. Opin. Plant Biol. 1: 240-244 (1998).

Bick JA, Setterdahl AT, Knaff DB, Chen Y, Pitcher LH, Zilinskas BA, Leustek T. Regulation of the plant-type 5'-adenylyl sulfate reductase by oxidative stress. Biochemistry 40: 9040-9048 (2001).

Bloom FR, Levin MS, Foor F, Tyler B. Regulation of glutamine synthetase formation in Escherichia coli: characterization of mutants lacking the uridylyltransferase. J. Bacteriol. 134: 569-577 (1978).

Brown JR, Masuchi Y, Robb FT, Doolittle WF. Evolutionary relationships of bacterial and archaeal glutamine synthetase genes. J. Mol. Evol. 38: 566-576 (1994).

Brown MS, Segal A, Stadtman ER. Modulation of glutamine synthetase adenylylation and deadenylylation is mediated by metabolic transformation of the P II -regulatory protein. Proc. Natl. Acad. Sci. U.S.A. 68: 2949-2953 (1971).

Bruggeman FJ, Boogerd FC, Westerhoff HV. The multifarious short-term regulation of ammonium assimilation of Escherichia coli: dissection using an in silico replica. FEBS J. 272: 1965-1985 (2005).

Bueno R, Pahel G, Magasanik B. Role of glnB and glnD gene products in regulation of the glnALG operon of Escherichia coli. J. Bacteriol. 164: 816-822 (1985).

Caban CE, Ginsburg A. Glutamine synthetase adenylyltransferase from Escherichia coli: purification and physical and chemical properties. Biochemistry 15: 1569-1580 (1976).

Carroll P, Pashley CA, Parish T. Functional analysis of GlnE, an essential adenylyl transferase in Mycobacterium tuberculosis. J. Bacteriol. 190: 4894-4902 (2008).

Chang C, Meyerowitz EM. Molecular cloning and DNA sequence of the Arabidopsis thaliana alcohol dehydrogenase gene. Proc. Natl. Acad. Sci. U.S.A. 83: 1408-1412 (1986).

Cheah E, Carr PD, Suffolk PM, Vasudevan SG, Dixon NE, Ollis DL. Structure of the Escherichia coli signal transducing protein PII. Structure 2: 981-990 (1994).

Chung HK, Rhee SG. Separation of glutamine synthetase species with different states of adenylylation by chromatography on monoclonal anti-AMP antibody affinity columns. Proc. Natl. Acad. Sci. U.S.A. 81: 4677-4681 (1984).

Coker JS, Vian A, Davies E. Identification, accumulation, and functional prediction of novel tomato transcripts systemically upregulated after fire damage. Physiol. Plant. 124: 311-322 (2005).

Colnaghi R, Rudnick P, He L, Green A, Yan D, Larson E, Kennedy C. Lethality of glnD null mutations in Azotobacter vinelandii is suppressible by prevention of glutamine synthetase adenylylation. Microbiology 147: 1267-1276 (2001).

Colombo G, Villafranca JJ. Amino acid sequence of Escherichia coli glutamine synthetase deduced from the DNA nucleotide sequence. J. Biol. Chem. 261: 10587-10591 (1986).

Dabrowski MJ, Dietze EC, Atkins WM. Engineering the aggregation properties of dodecameric glutamine synthetase: a single amino acid substitution controls 'salting out'. Protein Eng. 9: 291-298 (1996).

Dabrowski MJ, Yanchunas J Jr, Villafranca BC, Dietze EC, Schurke P, Atkins WM. Supramolecular self-assembly of glutamine synthetase: mutagenesis of a novel intermolecular metal binding site required for dodecamer stacking. Biochemistry 33: 14957-14964 (1994).

Dahl C. Insertional gene inactivation in a phototrophic sulphur bacterium: APS-reductase-deficient mutants of Chromatium vinosum. Microbiology 142: 3363-3372 (1996).

Dahlquist FW, Purich DL. Regulation of Escherichia coli glutamine synthetase. Evidence for the action of some feedback modifiers at the active site of the unadenylylated enzyme. Biochemistry 14: 1980-1989 (1975).

Dan H, Yang G, Zheng ZL. A negative regulatory role for auxin in sulphate deficiency response in Arabidopsis thaliana. Plant Mol. Biol. 63: 221-235 (2007).

Daugherty M, Polanuyer B, Farrell M, Scholle M, Lykidis A, de Crecy-Lagard V, Osterman A. Complete reconstitution of the human coenzyme A biosynthetic pathway via comparative genomics. J. Biol. Chem. 277: 21431-21439 (2002).

de Zamaroczy M, Delorme F, Elmerich C. Characterization of three different nitrogen-regulated promoter regions for the expression of glnB and glnA in Azospirillum brasilense. Mol. Gen. Genet. 224: 421-430 (1990).

de Zamaroczy M, Paquelin A, Peltre G, Forchhammer K, Elmerich C. Coexistence of two structurally similar but functionally different PII proteins in Azospirillum brasilense. J. Bacteriol. 178: 4143-4149 (1996).

Edwards R, Merrick M. The role of uridylyltransferase in the control of Klebsiella pneumoniae nif gene regulation. Mol. Gen. Genet. 247: 189-198 (1995).

Ely B, Amarasinghe AB, Bender RA. Ammonia assimilation and glutamate formation in Caulobacter crescentus. J. Bacteriol. 133: 225-230 (1978).

Emond D, Rondeau N, Cedergren RJ. Distinctive properties of glutamine synthetase from the cyanobacterium Anacystis nidulans. Can. J. Biochem. 57: 843-851 (1979).

Eom SJ, Ahn HJ, Kim HW, Baek SH, Suh SW. Crystallization and preliminary X-ray crystallographic studies of phosphopantetheine adenylyltransferase from Helicobacter pylori. Acta Crystallogr. D. Biol. Crystallogr. 59: 561-562 (2003).

Fink D, Falke D, Wohlleben W, Engels A. Nitrogen metabolism in Streptomyces coelicolor A3(2): modification of glutamine synthetase I by an adenylyltransferase. Microbiology 145: 2313-2322 (1999).

Fisher R, Tuli R, Haselkorn R. A cloned cyanobacterial gene for glutamine synthetase functions in Escherichia coli, but the enzyme is not adenylylated. Proc. Natl. Acad. Sci. U.S.A. 78: 3393-3397 (1981).

Fisher SH. Glutamine synthesis in Streptomyces--a review. Gene 115: 13-17 (1992).

Fisher SH, Wray LV Jr. Regulation of glutamine synthetase in Streptomyces coelicolor. J. Bacteriol. 171: 2378-2383 (1989).

Foor F, Cedergren RJ, Streicher SL, Rhee SG, Magasanik B. Glutamine synthetase of Klebsiella aerogenes: properties of glnD mutants lacking uridylyltransferase. J. Bacteriol. 134: 562-568 (1978).

Foor F, Janssen KA, Magasanik B. Regulation of synthesis of glutamine synthetase by adenylylated glutamine synthetase. Proc. Natl. Acad. Sci. U.S.A. 72: 4844-4848 (1975).

Foor F, Reuveny Z, Magasanik B. Regulation of the synthesis of glutamine synthetase by the PII protein in Klebsiella aerogenes. Proc. Natl. Acad. Sci. U.S.A. 77: 2636-2640 (1980).

Forchhammer K, Hedler A, Strobel H, Weiss V. Heterotrimerization of PII-like signalling proteins: implications for PII-mediated signal transduction systems. Mol. Microbiol. 33: 338-349 (1999).

Foster R, Thorner J, Martin GS. Nucleotidylation, not phosphorylation, is the major source of the phosphotyrosine detected in enteric bacteria. J. Bacteriol. 171: 272-279 (1989).

Foster WB, Griffith MJ, Kingdon HS. Affinity labeling of the active site of Escherichia coli glutamine synthetase by 5'-p-fluorosulfonylbenzoyladenosine. J. Biol. Chem. 256: 882-886 (1981).

Fritz G, Buchert T, Huber H, Stetter KO, Kroneck PMH. Adenylylsulfate reductases from archaea and bacteria are 1 : 1 alpha beta-heterodimeric iron-sulfur flavoenzymes - high similarity of molecular properties emphasizes their central role in sulfur metabolism. FEBS Lett. 473: 63-66 (2000).

Fulks RM, Stadtman ER. Regulation of glutamine synthetase, aspartokinase, and total protein turnover in Klebsiella aerogenes. Biochim. Biophys. Acta 843: 214-229 (1985).

Funanage VL, Brenchley JE. Characterization of Salmonella typhimurium mutants with altered glutamine synthetase activity. Genetics 86: 513-526 (1977).

Gaillardin CM, Magasanik B. Involvement of the product of the glnF gene in the autogenous regulation of glutamine synthetase formation in Klebsiella aerogenes. J. Bacteriol. 133: 1329-1338 (1978).

Gao Y, Schofield OM, Leustek T. Characterization of sulfate assimilation in marine algae focusing on the enzyme 5'-adenylylsulfate reductase. Plant Physiol. 123: 1087-1096 (2000).

Garcia E, Bancroft S, Rhee SG, Kustu S. The product of a newly identified gene, glnF, is required for synthesis of glutamine synthetase in Salmonella. Proc. Natl. Acad. Sci. U.S.A. 74: 1662-1666 (1977).

Garcia-Dominguez M, Reyes JC, Florencio FJ. Glutamine synthetase inactivation by protein-protein interaction. Proc. Natl. Acad. Sci. U.S.A. 96: 7161-7166 (1999).

Geerlof A, Lewendon A, Shaw WV. Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli. J. Biol. Chem. 274: 27105-27111 (1999).

Gerdes SY, Kurnasov OV, Shatalin K, Polanuyer B, Sloutsky R, Vonstein V, Overbeek R, Osterman AL. Comparative genomics of NAD biosynthesis in cyanobacteria. J. Bacteriol. 188: 3012-3023 (2006).

Gerdes SY, Scholle MD, D'Souza M, Bernal A, Baev MV, Farrell M, Kurnasov OV, Daugherty MD, Mseeh F, Polanuyer BM, Campbell JW, Anantha S, Shatalin KY, Chowdhury SA, Fonstein MY, Osterman AL. From genetic footprinting to antimicrobial drug targets: examples in cofactor biosynthetic pathways. J. Bacteriol. 184: 4555-4572 (2002).

Gill HS, Pfluegl GM, Eisenberg D. Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation. Biochemistry 41: 9863-9872 (2002).

Ginsburg A, Gorman EG, Neece SH, Blackburn MB. Thermodynamics of active-site ligand binding to Escherichia coli glutamine synthetase. Biochemistry 26: 5989-5996 (1987).

Hammarstrom A, Soliman A, Nordlund S. Low- and high-activity forms of glutamine synthetase from Rhodospirillum rubrum: sensitivity to feed-back effectors and activation of the low-activity form. Biochim. Biophys. Acta 1080: 259-263 (1991).

Harper C, Hayward D, Wiid I, van Helden P. Regulation of nitrogen metabolism in Mycobacterium tuberculosis: a comparison with mechanisms in Corynebacterium glutamicum and Streptomyces coelicolor. IUBMB Life 60: 643-650 (2008).

Harth G, Maslesa-Galic S, Tullius MV, Horwitz MA. All four Mycobacterium tuberculosis glnA genes encode glutamine synthetase activities but only GlnA1 is abundantly expressed and essential for bacterial homeostasis. Mol. Microbiol. 58: 1157-1172 (2005).

Hatzfeld Y, Lee S, Lee M, Leustek T, Saito K. Functional characterization of a gene encoding a fourth ATP sulfurylase isoform from Arabidopsis thaliana. Gene 248: 51-58 (2000).

Haverkamp T, Schwenn JD. Structure and function of a cysBJIH gene cluster in the purple sulphur bacterium Thiocapsa roseopersicina. Microbiology 145: 115-125 (1999).

Heacock AM, Foster DJ, Fisher SK. Prostanoid receptors regulate the volume-sensitive efflux of osmolytes from murine fibroblasts via a cyclic AMP-dependent mechanism. J. Pharmacol. Exp. Ther. 319: 963-971 (2006).

Hillemann D, Dammann T, Hillemann A, Wohlleben W. Genetic and biochemical characterization of the two glutamine synthetases GSI and GSII of the phosphinothricyl-alanyl-alanine producer, streptomyces viridochromogenes Tu494. J. Gen. Microbiol. 139: 1773-1783 (1993).

Hosted TJ, Rochefort DA, Benson DR. Close linkage of genes encoding glutamine synthetases I and II in Frankia alni CpI1. J. Bacteriol. 175: 3679-3684 (1993).

Hotter GS, Mouat P, Collins DM. Independent transcription of glutamine synthetase (glnA2) and glutamine synthetase adenylyltransferase (glnE) in Mycobacterium bovis and Mycobacterium tuberculosis Tuberculosis (Edinb.) 88: 382-389 (2008).

Ishino Y, Morgenthaler P, Hottinger H, Soll D. Organization and nucleotide sequence of the glutamine synthetase (glnA) gene from Lactobacillus delbrueckii subsp. bulgaricus. Appl. Environ. Microbiol. 58: 3165-3169 (1992).

Izard T. The crystal structures of phosphopantetheine adenylyltransferase with bound substrates reveal the enzyme's catalytic mechanism. J. Mol. Biol. 315: 487-495 (2002).

Izard T. A novel adenylate binding site confers phosphopantetheine adenylyltransferase interactions with coenzyme A. J. Bacteriol. 185: 4074-4080 (2003).

Izard T, Geerlof A. The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivity. EMBO J. 18: 2021-2030 (1999).

Izard T, Geerlof A, Lewendon A, Barker JJ. Cubic crystals of phosphopantetheine adenylyltransferase from Escherichia coli. Acta Crystallogr. D. Biol. Crystallogr. 55: 1226-1228 (1999).

Jackowski S, Rock CO. Metabolism of 4'-phosphopantetheine in Escherichia coli. J. Bacteriol. 158: 115-120 (1984).

Jaggi R, van Heeswijk WC, Westerhoff HV, Ollis DL, Vasudevan SG. The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction. EMBO J. 16: 5562-5571 (1997).

Jain A, Leustek T. A cDNA clone for 5'-adenylylphosphosulfate kinase from Arabidopsis thaliana. Plant Physiol. 105: 771-772 (1994).

Jakoby M, Kramer R, Burkovski A. Nitrogen regulation in Corynebacterium glutamicum: isolation of genes involved and biochemical characterization of corresponding proteins. FEMS Microbiol. Lett. 173: 303-310 (1999).

Jamai A, Gaillard C, Delrot S, Martinoia E. Dipeptide transport in barley mesophyll vacuoles. Planta 196: 430-433 (1995).

Janssen DB, Habets WJ, Marugg JT, Van Der Drift C. Nitrogen control in Pseudomonas aeruginosa: mutants affected in the synthesis of glutamine synthetase, urease, and NADP-dependent glutamate dehydrogenase. J. Bacteriol. 151: 22-28 (1982).

Janssen DB, op den Camp HJ, Leenen PJ, van der Drift C. The enzymes of the ammonia assimilation in Pseudomonas aeruginosa. Arch. Microbiol. 124: 197-203 (1980).

Jiang P, Mayo AE, Ninfa AJ. Escherichia coli glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49): kinetic characterization of regulation by PII, PII-UMP, glutamine, and alpha-ketoglutarate. Biochemistry 46: 4133-4146 (2007).

Jiang P, Ninfa AJ. Reconstitution of Escherichia coli glutamine synthetase adenylyltransferase from N-terminal and C-terminal fragments of the enzyme. Biochemistry 48: 415-423 (2009).

Jiang P, Ninfa AJ. Escherichia coli PII signal transduction protein controlling nitrogen assimilation acts as a sensor of adenylate energy charge in vitro. Biochemistry 46: 12979-12996 (2007).

Jiang P, Peliska JA, Ninfa AJ. The regulation of Escherichia coli glutamine synthetase revisited: role of 2-ketoglutarate in the regulation of glutamine synthetase adenylylation state. Biochemistry 37: 12802-12810 (1998).

Jiang P, Pioszak AA, Ninfa AJ. Structure-function analysis of glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49) of Escherichia coli. Biochemistry 46: 4117-4132 (2007).

Jiang P, Zucker P, Atkinson MR, Kamberov ES, Tirasophon W, Chandran P, Schefke BR, Ninfa AJ. Structure/function analysis of the PII signal transduction protein of Escherichia coli: genetic separation of interactions with protein receptors. J. Bacteriol. 179: 4342-4353 (1997).

Jiang P, Zucker P, Ninfa AJ. Probing interactions of the homotrimeric PII signal transduction protein with its receptors by use of PII heterotrimers formed in vitro from wild-type and mutant subunits. J. Bacteriol. 179: 4354-4360 (1997).

Johansson M, Nordlund S. Purification of P(II) and P(II)-UMP and in vitro studies of regulation of glutamine synthetase in Rhodospirillum rubrum. J. Bacteriol. 181: 6524-6529 (1999).

Jonsson A, Teixeira PF, Nordlund S. The activity of adenylyltransferase in Rhodospirillum rubrum is only affected by alpha-ketoglutarate and unmodified PII proteins, but not by glutamine, in vitro. FEBS J. 274: 2449-2460 (2007).

Kameya M, Arai H, Ishii M, Igarashi Y. Purification and properties of glutamine synthetase from Hydrogenobacter thermophilus TK-6. J. Biosci. Bioeng. 102: 311-315 (2006).

Kamnev AA, Antonyuk LP, Smirnova VE, Kulikov LA, Perfiliev YD, Kudelina IA, Kuzmann E, Vertes A. Structural characterization of glutamine synthetase from Azospirillum brasilense. Biopolymers 74: 64-68 (2004).

Kappler U, Dahl C. Enzymology and molecular biology of prokaryotic sulfite oxidation. FEMS Microbiol. Lett. 203: 1-9 (2001).

Kim IH, Kwak SJ, Kang J, Park SC. Transcriptional control of the glnD gene is not dependent on nitrogen availability in Escherichia coli. Mol. Cells 8: 483-490 (1998).

Kimura K, Kaizu Y, Matsuoka K, Nakano Y. The conversion of native adenylylated glutamine synthetase into phosphotyrosine enzyme by micrococcal nuclease. Biochem. Biophys. Res. Commun. 137: 716-721 (1986).

Kimura K, Matsuoka K, Kobayashi H. Regulation and properties of the glutamine synthetase purified from Photobacterium phosphoreum. J. Biochem. (Tokyo) 99: 111-117 (1986).

Kimura K, Nakano Y, Matsuoka K. O-Phosphotyrosyl glutamine synthetase: modification of the nucleotide ligation site of adenylylated glutamine synthetase. J. Biochem. (Tokyo) 105: 84-87 (1989).

Kimura K, Sugano S, Funae A, Nakano Y. Characterization of Bacillus subtilis glutamine synthetase by limited proteolysis. J. Biochem. (Tokyo) 110: 526-531 (1991).

Kimura K, Suzuki H, Nakano Y. Regulation of glutamine synthetase activity by phosphorylation instead of by adenylylation. Biochem. Biophys. Res. Commun. 155: 1133-1138 (1988).

Kimura K, Yagi K, Matsuoka K. Regulation of Mycobacterium smegmatis glutamine synthetase by adenylylation. J. Biochem. (Tokyo) 95: 1559-1567 (1984).

Kleinschmidt JA, Kleiner D. The glutamine synthetase from Azotobacter vinelandii: purification, characterization, regulation and localization. Eur. J. Biochem. 89: 51-60 (1978).

Kremeckova H, Svrcula B, Mikes V. Purification and some properties of glutamate dehydrogenase and glutamine synthetase from Paracoccus denitrificans. J. Gen. Microbiol. 138: 1587-1591 (1992).

Krone FA, Westphal G, Schwenn JD. Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli. Mol. Gen. Genet. 225: 314-319 (1991).

Krupa A, Sandhya K, Srinivasan N, Jonnalagadda S. A conserved domain in prokaryotic bifunctional FAD synthetases can potentially catalyze nucleotide transfer. Trends Biochem. Sci. 28: 9-12 (2003).

Kupke T, Hernandez-Acosta P, Culianez-Macia FA. 4'-Phosphopantetheine and coenzyme A biosynthesis in plants. J. Biol. Chem. 278: 38229-38237 (2003).

Kustu S, Hirschman J, Burton D, Jelesko J, Meeks JC. Covalent modification of bacterial glutamine synthetase: physiological significance. Mol. Gen. Genet. 197: 309-317 (1984).

Kustu SG, McKereghan K. Mutations affecting glutamine synthetase activity in Salmonella typhimurium. J. Bacteriol. 122: 1006-1016 (1975).

Lee S, Leustek T. APS kinase from Arabidopsis thaliana: genomic organization, expression, and kinetic analysis of the recombinant enzyme. Biochem. Biophys. Res. Commun. 247: 171-175 (1998).

Lepo JE, Stacey G, Wyss O, Tabita FR. The purification of glutamine synthetase from Azotobacter and other procaryotes by blue sepharose chromatography. Biochim. Biophys. Acta 568: 428-436 (1979).

Leustek T, Saito K. Sulfate transport and assimilation in plants. Plant Physiol. 120: 637-644 (1999).

Levine RL. Oxidative modification of glutamine synthetase. II. Characterization of the ascorbate model system. J. Biol. Chem. 258: 11828-11833 (1983).

Li C, Peck HD Jr, Przybyla AE. Cloning of the 3'-phosphoadenylyl sulfate reductase and sulfite reductase genes from Escherichia coli K-12. Gene 53: 227-234 (1987).

Liaw SH, Jun G, Eisenberg D. Interactions of nucleotides with fully unadenylylated glutamine synthetase from Salmonella typhimurium. Biochemistry 33: 11184-11188 (1994).

Liaw SH, Pan C, Eisenberg D. Feedback inhibition of fully unadenylylated glutamine synthetase from Salmonella typhimurium by glycine, alanine, and serine. Proc. Natl. Acad. Sci. U.S.A. 90: 4996-5000 (1993).

Lillig CH, Prior A, Schwenn JD, Aslund F, Ritz D, Vlamis-Gardikas A, Holmgren A. New thioredoxins and glutaredoxins as electron donors of 3'-phosphoadenylylsulfate reductase. J. Biol. Chem. 274: 7695-7698 (1999).

Little R, Colombo V, Leech A, Dixon R. Direct interaction of the NifL regulatory protein with the GlnK signal transducer enables the Azotobacter vinelandii NifL-NifA regulatory system to respond to conditions replete for nitrogen. J. Biol. Chem. 277: 15472-15481 (2002).

Loeffler C, Berger S, Guy A, Durand T, Bringmann G, Dreyer M, von Rad U, Durner J, Mueller MJ. B1-phytoprostanes trigger plant defense and detoxification responses. Plant Physiol. 137: 328-340 (2005).

Luo S, Kim G, Levine RL. Mutation of the adenylylated tyrosine of glutamine synthetase alters its catalytic properties. Biochemistry 44: 9441-9446 (2005).

MacRae IJ, Rose AB, Segel IH. Adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum. site-directed mutagenesis at putative phosphoryl-accepting and ATP P-loop residues. J. Biol. Chem. 273: 28583-28589 (1998).

Mangum JH, Magni G, Stadtman ER. Regulation of glutamine synthetase adenylylation and deadenylylation by the enzymatic uridylylation and deuridylylation of the PII regulatory protein. Arch. Biochem. Biophys. 158: 514-525 (1973).

Masuda S, Ono TA. Biochemical characterization of the major adenylyl cyclase, Cya1, in the cyanobacterium Synechocystis sp. PCC 6803. FEBS Lett. 577: 255-258 (2004).

Maurizi MR, Ginsburg A. Reactivation of glutamine synthetase from Escherichia coli after auto-inactivation with L-methionine-S-sulfoximine, ATP, and Mn2+. J. Biol. Chem. 257: 4271-4278 (1982).

Maurizi MR, Ginsburg A. Adenosine 5'-triphosphate analogues as structural probes for Escherichia coli glutamine synthetase. Biochemistry 25: 131-140 (1986).

McCoy JG, Arabshahi A, Bitto E, Bingman CA, Ruzicka FJ, Frey PA, Phillips GN Jr. Structure and mechanism of an ADP-glucose phosphorylase from Arabidopsis thaliana. Biochemistry 45: 3154-3162 (2006).

Mehta R, Pearson JT, Mahajan S, Nath A, Hickey MJ, Sherman DR, Atkins WM. Adenylylation and catalytic properties of Mycobacterium tuberculosis glutamine synthetase expressed in Escherichia coli versus mycobacteria. J. Biol. Chem. 279: 22477-22482 (2004).

Merida A, Candau P, Florencio FJ. Regulation of glutamine synthetase activity in the unicellular cyanobacterium Synechocystis sp. strain PCC 6803 by the nitrogen source: effect of ammonium. J. Bacteriol. 173: 4095-4100 (1991).

Merida A, Candau P, Florencio FJ. In vitro reactivation of in vivo ammonium-inactivated glutamine synthetase from Synechocystis sp. PCC 6803. Biochem. Biophys. Res. Commun. 181: 780-786 (1991).

Meyer JM, Stadtman ER. Glutamine synthetase of pseudomonads: some biochemical and physicochemical properties. J. Bacteriol. 146: 705-712 (1981).

Meyer JM, Stadtman ER. Adenylylation state of glutamine synthetase and permeability properties of Pseudomonas fluorescens. Arch. Biochem. Biophys. 246: 622-632 (1986).

Michel-Reydellet N, Desnoues N, Elmerich C, Kaminski PA. Characterization of Azorhizobium caulinodans glnB and glnA genes: involvement of the P(II) protein in symbiotic nitrogen fixation. J. Bacteriol. 179: 3580-3587 (1997).

Michel-Reydellet N, Kaminski PA. Azorhizobium caulinodans PII and GlnK proteins control nitrogen fixation and ammonia assimilation. J. Bacteriol. 181: 2655-2658 (1999).

Montoya G, Svensson C, Savage H, Schwenn JD, Sinning I. Crystallization and preliminary X-ray diffraction studies of phospho-adenylylsulfate (PAPS) reductase from E. coli. Acta Crystallogr. D. Biol. Crystallogr. 54: 281-283 (1998).

Munoz-Centeno MC, Cejudo FJ, Paneque A. In vivo modification of Azotobacter chroococcum glutamine synthetase. Biochem. J. 298: 641-645 (1994).

Mura U, Stadtman ER. Glutamine synthetase adenylylation in permeabilized cells of Escherichia coli. J. Biol. Chem. 256: 13014-13021 (1981).

Mutalik VK, Shah P, Venkatesh KV. Allosteric interactions and bifunctionality make the response of glutamine synthetase cascade system of Escherichia coli robust and ultrasensitive. J. Biol. Chem. 278: 26327-26332 (2003).

Nakamura K, Stadtman ER. Oxidative inactivation of glutamine synthetase subunits. Proc. Natl. Acad. Sci. U.S.A. 81: 2011-2015 (1984).

Nandineni MR, Laishram RS, Gowrishankar J. Osmosensitivity associated with insertions in argP (iciA) or glnE in glutamate synthase-deficient mutants of Escherichia coli. J. Bacteriol. 186: 6391-6399 (2004).

Niehaus A, Gisselmann G, Schwenn JD. Primary structure of the Synechococcus PCC 7942 PAPS reductase gene. Plant Mol. Biol. 20: 1179-1183 (1992).

Nolden L, Farwick M, Kramer R, Burkovski A. Glutamine synthetases of Corynebacterium glutamicum: transcriptional control and regulation of activity. FEMS Microbiol. Lett. 201: 91-98 (2001).

Ntefidou M, Iseki M, Watanabe M, Lebert M, Hader DP. Photoactivated adenylyl cyclase controls phototaxis in the flagellate Euglena gracilis. Plant Physiol. 133: 1517-1521 (2003).

Orr J, Haselkorn R. Regulation of glutamine synthetase activity and synthesis in free-living and symbiotic Anabaena spp. J. Bacteriol. 152: 626-635 (1982).

Orr J, Keefer LM, Keim P, Nguyen TD, Wellems T, Heinrikson RL, Haselkorn R. Purification, physical characterization, and NH2-terminal sequence of glutamine synthetase from the cyanobacterium Anabaena 7120. J. Biol. Chem. 256: 13091-13098 (1981).

Parent CA, Devreotes PN. Molecular genetics of signal transduction in Dictyostelium. Annu. Rev. Biochem. 65: 411-440 (1996).

Pashley CA, Brown AC, Robertson D, Parish T. Identification of the Mycobacterium tuberculosis GlnE promoter and its response to nitrogen availability. Microbiology 152: 2727-2734 (2006).

Penyige A, Kalmanczhelyi A, Sipos A, Ensign JC, Barabas G. Modification of glutamine synthetase in Streptomyces griseus by ADP-ribosylation and adenylylation. Biochem. Biophys. Res. Commun. 204: 598-605 (1994).

Persuhn DC, Souza EM, Steffens MB, Pedrosa FO, Yates MG, Rigo LU. The transcriptional activator NtrC controls the expression and activity of glutamine synthetase in Herbaspirillum seropedicae. FEMS Microbiol. Lett. 192: 217-221 (2000).

Pesole G, Gissi C, Lanave C, Saccone C. Glutamine synthetase gene evolution in bacteria. Mol. Biol. Evol. 12: 189-197 (1995).

Phartiyal P, Kim WS, Cahoon RE, Jez JM, Krishnan HB. The role of 5'-adenylylsulfate reductase in the sulfur assimilation pathway of soybean: molecular cloning, kinetic characterization, and gene expression. Phytochemistry 69: 356-364 (2008).

Pinkofsky HB, Ginsburg A, Reardon I, Heinrikson RL. Lysyl residue 47 is near the subunit ATP-binding site of glutamine synthetase from Escherichia coli. J. Biol. Chem. 259: 9616-9622 (1984).

Pons G, Raefsky-Estrin C, Carothers DJ, Pepin RA, Javed AA, Jesse BW, Ganapathi MK, Samols D, Patel MS. Cloning and cDNA sequence of the dihydrolipoamide dehydrogenase component human alpha-ketoacid dehydrogenase complexes. Proc. Natl. Acad. Sci. U.S.A. 85: 1422-1426 (1988).

Prior A, Uhrig JF, Heins L, Wiesmann A, Lillig CH, Stoltze C, Soll J, Schwenn JD. Structural and kinetic properties of adenylyl sulfate reductase from Catharanthus roseus cell cultures. Biochim. Biophys. Acta 1430: 25-38 (1999).

Rato C, Monteiro D, Hepler PK, Malho R. Calmodulin activity and cAMP signalling modulate growth and apical secretion in pollen tubes. Plant J. 38: 887-897 (2004).

Ravina CG, Chang CI, Tsakraklides GP, McDermott JP, Vega JM, Leustek T, Gotor C, Davies JP. The sac mutants of Chlamydomonas reinhardtii reveal transcriptional and posttranscriptional control of cysteine biosynthesis. Plant Physiol. 130: 2076-2084 (2002).

Read R, Pashley CA, Smith D, Parish T. The role of GlnD in ammonia assimilation in Mycobacterium tuberculosis. Tuberculosis (Edinb.) 87: 384-390 (2007).

Reitzer L. Nitrogen assimilation and global regulation in Escherichia coli. Annu. Rev. Microbiol. 57: 155-176 (2003).

Reuther J, Wohlleben W. Nitrogen metabolism in Streptomyces coelicolor: transcriptional and post-translational regulation. J. Mol. Microbiol. Biotechnol. 12: 139-146 (2007).

Reuveny Z, Foor F, Magasanik B. Regulation of glutamine synthetase by regulatory protein PII in Klebsiella aerogenes mutants lacking adenylyltransferase. J. Bacteriol. 146: 740-745 (1981).

Rexer HU, Schaberle T, Wohlleben W, Engels A. Investigation of the functional properties and regulation of three glutamine synthetase-like genes in Streptomyces coelicolor A3(2). Arch. Microbiol. 186: 447-458 (2006).

Reynaldo LP, Villafranca JJ, Horrocks WD Jr. Investigating the effects of posttranslational adenylylation on the metal binding sites of Escherichia coli glutamine synthetase using lanthanide luminescence spectroscopy. Protein Sci. 5: 2532-2544 (1996).

Rhee SG, Chock PB. Mechanistic studies of glutamine synthetase from Escherichia coli: kinetic evidence for two reaction intermediates in biosynthetic reaction. Proc. Natl. Acad. Sci. U.S.A. 73: 476-480 (1976).

Rhee SG, Chock PB, Stadtman ER. Mechanistic studies of glutamine synthetase from Escherichia coli. An integrated mechanism for biosynthesis, transferase, ATPase reaction. Biochimie 58: 35-49 (1976).

Rhee SG, Chock PB, Wedler FC, Sugiyama Y. Subunit interaction in unadenylylated glutamine synthetase from Escherichia coli. Evidence from methionine sulfoximine inhibition studies. J. Biol. Chem. 256: 644-648 (1981).

Rhee SG, Park SC, Koo JH. The role of adenylyltransferase and uridylyltransferase in the regulation of glutamine synthetase in Escherichia coli. Curr. Top. Cell Regul. 27: 221-232 (1985).

Rhee SG, Ubom GA, Hunt JB, Chock PB. Catalytic cycle of the biosynthetic reaction catalyzed by adenylylated glutamine synthetase from Escherichia coli. J. Biol. Chem. 257: 289-297 (1982).

Rhee SG, Ubom GA, Hunt JB, Chock PB. Fluorometric studies of aza-epsilon-adenylylated glutamine synthetase from Escherichia coli. J. Biol. Chem. 256: 6010-6016 (1981).

Rivett AJ. Preferential degradation of the oxidatively modified form of glutamine synthetase by intracellular mammalian proteases. J. Biol. Chem. 260: 300-305 (1985).

Rivett AJ, Roseman JE, Oliver CN, Levine RL, Stadtman ER. Covalent modification of proteins by mixed-function oxidation: recognition by intracellular proteases. Prog. Clin. Biol. Res. 180: 317-328 (1985).

Rotte C, Leustek T. Differential subcellular localization and expression of ATP sulfurylase and 5'-adenylylsulfate reductase during ontogenesis of Arabidopsis leaves indicates that cytosolic and plastid forms of ATP sulfurylase may have specialized functions. Plant Physiol. 124: 715-724 (2000).

Rubio S, Whitehead L, Larson TR, Graham IA, Rodriguez PL. The coenzyme A biosynthetic enzyme phosphopantetheine adenylyltransferase plays a crucial role for plant growth, salt/osmotic-stress resistance and seed lipid storage. Plant Physiol. 148: 546-556 (2008).

Rudnick P, Kunz C, Gunatilaka MK, Hines ER, Kennedy C. Role of GlnK in NifL-mediated regulation of NifA activity in Azotobacter vinelandii. J. Bacteriol. 184: 812-820 (2002).

Savage H, Montoya G, Svensson C, Schwenn JD, Sinning I. Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases. Structure 5: 895-906 (1997).

Schwenn JD, Krone FA, Husmann K. Yeast PAPS reductase: properties and requirements of the purified enzyme. Arch. Microbiol. 150: 313-319 (1988).

Senior PJ. Regulation of nitrogen metabolism in Escherichia coli and Klebsiella aerogenes: studies with the continuous-culture technique. J. Bacteriol. 123: 407-418 (1975).

Setya A, Murillo M, Leustek T. Sulfate reduction in higher plants: molecular evidence for a novel 5'-adenylylsulfate reductase. Proc. Natl. Acad. Sci. U.S.A. 93: 13383-13388 (1996).

Shaltiel S, Adler SP, Purich D, Caban C, Senior P, Stadtman ER. Omega-aminoalkyl agaroses in the resolution of enzymes involved in regulation of glutamine metabolism. Proc. Natl. Acad. Sci. U.S.A. 72: 3397-3401 (1975).

Shapiro BM, Kingdon HS, Stadtman ER. Regulation of glutamine synthetase. VII. Adenylyl glutamine synthetase: a new form of the enzyme with altered regulatory and kinetic properties. Proc. Natl. Acad. Sci. U.S.A. 58: 642-649 (1967).

Shapiro BM, Stadtman ER. 5'-Adenylyl-O-tyrosine. The novel phosphodiester residue of adenylylated glutamine synthetase from Escherichia coli. J. Biol. Chem. 243: 3769-3771 (1968).

Shu S, Mahadeo DC, Liu X, Liu W, Parent CA, Korn ED. S-Adenosylhomocysteine hydrolase is localized at the front of chemotaxing cells, suggesting a role for transmethylation during migration. Proc. Natl. Acad. Sci. U.S.A. 103: 19788-19793 (2006).

Son HS, Rhee SG. Cascade control of Escherichia coli glutamine synthetase. Purification and properties of PII protein and nucleotide sequence of its structural gene. J. Biol. Chem. 262: 8690-8695 (1987).

Srivastava A, Tripathi AK. Adenosine diphosphate ribosylation of dinitrogenase reductase and adenylylation of glutamine synthetase control ammonia excretion in ethylenediamine-resistant mutants of Azospirillum brasilense Sp7. Curr. Microbiol. 53: 317-323 (2006).

Stadtman ER, Hohman RJ, Davis JN, Wittenberger M, Chock PB, Rhee SG. Subunit interaction of adenylylated glutamine synthetase. Mol. Biol. Biochem. Biophys. 32: 144-156 (1980).

Stokes BO, Boyer PD. Rapid transfer of oxygens from inorganic phosphate to glutamine catalyzed by Escherichia coli glutamine synthetase. J. Biol. Chem. 251: 5558-5564 (1976).

Streicher SL, Tyler B. Regulation of glutamine synthetase activity by adenylylation in the Gram-positive bacterium Streptomyces cattleya. Proc. Natl. Acad. Sci. U.S.A. 78: 229-233 (1981).

Strosser J, Ludke A, Schaffer S, Kramer R, Burkovski A. Regulation of GlnK activity: modification, membrane sequestration and proteolysis as regulatory principles in the network of nitrogen control in Corynebacterium glutamicum. Mol. Microbiol. 54: 132-147 (2004).

Tahiliani AG, Beinlich CJ. Pantothenic acid in health and disease. Vitam. Horm. 46: 165-228 (1991).

Thomas D, Barbey R, Surdin-Kerjan Y. Gene-enzyme relationship in the sulfate assimilation pathway of Saccharomyces cerevisiae. Study of the 3'-phosphoadenylylsulfate reductase structural gene. J. Biol. Chem. 265: 15518-15524 (1990).

Todhunter JA, Purich DL. Use of the sodium borohydride reduction technique to identify a gamma-glutamyl phosphate intermediary in the Escherichia coli glutamine synthetase reaction. J. Biol. Chem. 250: 3505-3509 (1975).

Torchia C, Takagi Y, Ho CK. Archaeal RNA ligase is a homodimeric protein that catalyzes intramolecular ligation of single-stranded RNA and DNA. Nucleic Acids Res. 36: 6218-6227 (2008).

Tsakraklides G, Martin M, Chalam R, Tarczynski MC, Schmidt A, Leustek T. Sulfate reduction is increased in transgenic Arabidopsis thaliana expressing 5'-adenylylsulfate reductase from Pseudomonas aeruginosa. Plant J. 32: 879-889 (2002).

Ubom GA, Hunt JB, Timmons RB. Spin-labeled analogues of ATP, ADP and AMP: substitutes for normal nucleotides in biochemical systems. Biochim. Biophys. Acta 997: 1-8 (1989).

Upchurch RG, Elkan GH. The role of ammonia, L-glutamate, and cyclic adenosine 3',5'-monophosphate in the regulation of ammonia assimilation in Rhizobium japonicum. Biochim. Biophys. Acta 538: 244-248 (1978).

Ureta A, Nordlund S. Glutamine synthetase from Acetobacter diazotrophicus: properties and regulation. FEMS Microbiol. Lett. 202: 177-180 (2001).

Uria-Nickelsen MR, Leadbetter ER, Godchaux W 3d. Sulfonate-sulfur assimilation by yeasts resembles that of bacteria. FEMS Microbiol. Lett. 114: 73-77 (1993).

Van Dommelen A, Spaepen S, Vanderleyden J. Identification of the glutamine synthetase adenylyltransferase of Azospirillum brasilense. Res. Microbiol. 160: 205-212 (2009).

van Heeswijk WC, Hoving S, Molenaar D, Stegeman B, Kahn D, Westerhoff HV. An alternative PII protein in the regulation of glutamine synthetase in Escherichia coli. Mol. Microbiol. 21: 133-146 (1996).

van Heeswijk WC, Rabenberg M, Westerhoff HV, Kahn D. The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli. Mol. Microbiol. 9: 443-457 (1993).

van Heeswijk WC, Stegeman B, Hoving S, Molenaar D, Kahn D, Westerhoff HV. An additional PII in Escherichia coli: a new regulatory protein in the glutamine synthetase cascade. FEMS Microbiol. Lett. 132: 153-157 (1995).

van Heeswijk WC, Wen D, Clancy P, Jaggi R, Ollis DL, Westerhoff HV, Vasudevan SG. The Escherichia coli signal transducers PII (GlnB) and GlnK form heterotrimers in vivo: fine tuning the nitrogen signal cascade. Proc. Natl. Acad. Sci. U.S.A. 97: 3942-3947 (2000).

Varon-Castellanos R, Havsteen BH, Garcia-Moreno M, Valero-Ruiz E, Molina-Alarcon M, Garcia-Canovas F. Time course of the uridylylation and adenylylation states in the glutamine synthetase bicyclic cascade. Biochem. J. 294: 813-819 (1993).

Villafranca JJ, Ash DE, Wedler FC. Manganese(II) and substrate interaction with unadenylylated glutamine synthetase (Escherichia coli w). I. Temperature and frequency dependent nuclear magnetic resonance studies. Biochemistry 15: 536-543 (1976).

Wedler FC, Shreve DS, Kenney RM, Ashour AE, Carfi J, Rhee SG. Two glutamine synthetases from Bacillus caldolyticus, an extreme thermophile. Isolation, physicochemical and kinetic properties. J. Biol. Chem. 255: 9507-9516 (1980).

Willard FS, Kimple RJ, Siderovski DP. Return of the GDI: the GoLoco motif in cell division. Annu. Rev. Biochem. 73: 925-951 (2004).

Witmer MR, Palmieri-Young D, Villafranca JJ. Probing the catalytic roles of n2-site glutamate residues in Escherichia coli glutamine synthetase by mutagenesis. Protein Sci. 3: 1746-1759 (1994).

Woehle DL, Lueddecke BA, Ludden PW. ATP-dependent and NAD-dependent modification of glutamine synthetase from Rhodospirillum rubrum in vitro. J. Biol. Chem. 265: 13741-13749 (1990).

Worrall DM, Tubbs PK. A bifunctional enzyme complex in coenzyme A biosynthesis: purification of pantetheine phosphate adenylyltransferase and dephospho-CoA kinase. Biochem. J. 215: 153-157 (1983).

Wray LV Jr, Atkinson MR, Fisher SH. Identification and cloning of the glnR locus, which is required for transcription of the glnA gene in Streptomyces coelicolor A3(2). J. Bacteriol. 173: 7351-7360 (1991).

Xia TH, Jiao RS. Studies on glutamine synthetase from Streptomyces hygroscopicus var. jinggangensis. Sci. Sin. [B] 29: 379-388 (1986).

Xu Y, Wen D, Brown C, Chen CJ, Carr PD, Ollis DL, Vasudevan SG. Expression, purification and crystallization of the C-terminal domain of Escherichia coli adenylyltransferase. Acta Crystallograph. Sect. F. Struct. Biol. Cryst. Commun. 61: 663-665 (2005).

Xu Y, Zhang R, Joachimiak A, Carr PD, Huber T, Vasudevan SG, Ollis DL. Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase. Structure (Camb.) 12: 861-869 (2004).

Xu YB, Wen DY, Clancy P, Carr PD, Ollis DL, Vasudevan SG. Expression, purification, crystallization, and preliminary X-ray analysis of the N-terminal domain of Escherichia coli adenylyl transferase. Protein Expr. Purif. 34: 142-146 (2004).

Yagi T, Ogata M. Catalytic properties of adenylylsulfate reductase from Desulfovibrio vulgaris Miyazaki. Biochimie 78: 838-846 (1996).

Yamamoto S, Wakayama M, Tachiki T. Cloning and expression of Pseudomonas taetrolens Y-30 gene encoding glutamine synthetase: an enzyme available for theanine production by coupled fermentation with energy transfer. Biosci. Biotechnol. Biochem. 70: 500-507 (2006).

Yan D, Ikeda TP, Shauger AE, Kustu S. Glutamate is required to maintain the steady-state potassium pool in Salmonella typhimurium. Proc. Natl. Acad. Sci. U.S.A. 93: 6527-6531 (1996).

Yin ZM, Chen QY, Sima J, Wu YF, Zhang SQ. The expression regulation and characterization of glutamine synthetase from the hyperthermoacidophilic crenarcheon Sulfolobus acidocaldarius. Prog. Biochem. Biophys. 30: 767-771 (2003).

Zhang Y, Pohlmann EL, Conrad MC, Roberts GP. The poor growth of Rhodospirillum rubrum mutants lacking PII proteins is due to an excess of glutamine synthetase activity. Mol. Microbiol. 61: 497-510 (2006).

Zhang Y, Pohlmann EL, Ludden PW, Roberts GP. Mutagenesis and functional characterization of the glnB, glnA, and nifA genes from the photosynthetic bacterium Rhodospirillum rubrum. J. Bacteriol. 182: 983-992 (2000).

Zhang Y, Pohlmann EL, Roberts GP. GlnD is essential for NifA activation, NtrB/NtrC-regulated gene expression, and posttranslational regulation of nitrogenase activity in the photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. J. Bacteriol. 187: 1254-1265 (2005).

Zhao L, Allanson NM, Thomson SP, Maclean JK, Barker JJ, Primrose WU, Tyler PD, Lewendon A. Inhibitors of phosphopantetheine adenylyltransferase. Eur. J. Med. Chem. 38: 345-349 (2003).

Zhyvoloup A, Nemazanyy I, Babich A, Panasyuk G, Pobigailo N, Vudmaska M, Naidenov V, Kukharenko O, Palchevskii S, Savinska L, Ovcharenko G, Verdier F, Valovka T, Fenton T, Rebholz H, Wang ML, Shepherd P, Matsuka G, Filonenko V, Gout IT. Molecular cloning of CoA Synthase. The missing link in CoA biosynthesis. J. Biol. Chem. 277: 22107-22110 (2002).

Number of references = 231

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