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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
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References
HORT640 - Metabolic Plant Physiology

References, proline dehydrogenase

Abraham E, Rigo G, Szekely G, Nagy R, Koncz C, Szabados L. Light-dependent induction of proline biosynthesis by abscisic acid and salt stress is inhibited by brassinosteroid in Arabidopsis. Plant Mol. Biol. 51: 363-372 (2003).

Abrahamson JL, Baker LG, Stephenson JT, Wood JM. Proline dehydrogenase from Escherichia coli K12. Properties of the membrane-associated enzyme. Eur. J. Biochem. 134: 77-82 (1983).

Ambard-Bretteville F, Sorin C, Rebeille F, Hourton-Cabassa C, Colas des Francs-Small C. Repression of formate dehydrogenase in Solanum tuberosum increases steady-state levels of formate and accelerates the accumulation of proline in response to osmotic stress. Plant Mol. Biol. 52: 1153-1168 (2003).

Ankri S, Serebrijski I, Reyes O, Leblon G. Mutations in the Corynebacterium glutamicum proline biosynthetic pathway: a natural bypass of th proA step. J. Bacteriol. 178: 4412-4419 (1996).

Ayliffe MA, Mitchell HJ, Deuschle K, Pryor AJ. Comparative analysis in cereals of a key proline catabolism gene. Mol. Genet. Genomics 274: 494-505 (2005).

Baich A. The biosynthesis of proline in Escherichia coli. Phosphate-dependent glutamate gamma-semialdehyde dehydrogenase (NADP), the second enzyme in the pathway. Biochim. Biophys. Acta 244: 129-134 (1971).

Balboni E, Hecht RI. Studies on the inner mitochondrial membrane localization of proline dehydrogenase. Biochim. Biophys. Acta 462: 171-176 (1977).

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

Becker DF, Thomas EA. Redox properties of the PutA protein from Escherichia coli and the influence of the flavin redox state on PutA-DNA interactions. Biochemistry 40: 4714-4721 (2001).

Belitsky BR, Sonenshein AL. Modulation of activity of Bacillus subtilis regulatory proteins GltC and TnrA by glutamate dehydrogenase. J. Bacteriol. 186: 3399-3407 (2004).

Blake RL, Hall JG, Russell ES. Mitochondrial proline dehydrogenase deficiency in hyperprolinemic PRO/Re mice: genetic and enzymatic analyses. Biochem. Genet. 14: 739-757 (1976).

Blumenthal KM, Moon K, Smith EL. Nicotinamide adenine dinucleotide phosphate-specific glutamate dehydrogenase of Neurospora. J. Biol. Chem. 250: 3644-3654 (1975).

Bon EP, Carvajal E, Stanbrough M, Rowen D, Magasanik B. Asparaginase II of Saccharomyces cerevisiae. GLN3/URE2 regulation of a periplasmic enzyme. Appl. Biochem. Biotechnol. 63-65: 203-212 (1997).

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).

Brandriss MC, Magasanik B. Genetics and physiology of proline utilization in Saccharomyces cerevisiae: mutation causing constitutive enzyme expression. J. Bacteriol. 140: 504-507 (1979).

Brandriss MC, Magasanik B. Proline: an essential intermediate in arginine degradation in Saccharomyces cerevisiae. J. Bacteriol. 143: 1403-1410 (1980).

Brandriss MC, Magasanik B. Genetics and physiology of proline utilization in Saccharomyces cerevisiae: enzyme induction by proline. J. Bacteriol. 140: 498-503 (1979).

Brandriss MC, Magasanik B. Subcellular compartmentation in control of converging pathways for proline and arginine metabolism in Saccharomyces cerevisiae. J. Bacteriol. 145: 1359-1364 (1981).

Broach J, Neumann C, Kustu S. Mutant strains (nit) of Salmonella typhimurium with a pleiotropic defect in nitrogen metabolism. J. Bacteriol. 128: 86-98 (1976).

Brown ED, Wood JM. Conformational change and membrane association of the PutA protein are coincident with reduction of its FAD cofactor by proline. J. Biol. Chem. 268: 8972-8979 (1993).

Brown ED, Wood JM. Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli. J. Biol. Chem. 267: 13086-13092 (1992).

Camacho Barron M, Gonzalez de Mejia E. Comparative study of enzymes related to proline metabolism in tepary bean (Phaseolus acutifolius) and common bean (Phaseolus vulgaris) under drought and irrigated conditions, and various urea concentrations. Plant Foods Hum. Nutr. 52: 119-132 (1998).

Chang YC, Lee TM. High temperature-induced free proline accumulation in Gracilaria tenuistipitata (Rhodophyta). Bot. Bul. Acad. Sin. 40: 289-294 (1999).

Chen CT, Chen LM, Lin CC, Kao CH. Regulation of proline accumulation in detached rice leaves exposed to excess copper. Plant Sci. 160: 283-290 (2001).

Chen TH, Murata N. Enhancement of tolerance of abiotic stress by metabolic engineering of betaines and other compatible solutes. Curr. Opin. Plant Biol. 5: 250-257 (2002).

Chen Z, Hong X, Zhang H, Wang Y, Li X, Zhu JK, Gong Z. Disruption of the cellulose synthase gene, AtCesA8/IRX1, enhances drought and osmotic stress tolerance in Arabidopsis. Plant J. 43: 273-283 (2005).

Cho K, Winans SC. The putA gene of Agrobacterium tumefaciens is transcriptionally activated in response to proline by an Lrp-like protein and is not autoregulated. Mol. Microbiol. 22: 1025-1033 (1996).

Clancy M, Madill KA, Wood JM. Genetic and biochemical requirements for chemotaxis to L-proline in Escherichia coli. J. Bacteriol. 146: 902-906 (1981).

Conjard A, Komaty O, Delage H, Boghossian M, Martin M, Ferrier B, Baverel G. Inhibition of glutamine synthetase in the mouse kidney - A novel mechanism of adaptation to metabolic acidosis. J. Biol. Chem. 278: 38159-38166 (2003).

Costilow RN, Cooper D. Identity of proline dehydrogenase and delta1-pyrroline-5-carboxylic acid reductase in Clostridium sporogenes. J. Bacteriol. 134: 139-146 (1978).

Courchesne WE, Magasanik B. Ammonia regulation of amino acid permeases in Saccharomyces cerevisiae. Mol. Cell Biol. 3: 672-683 (1983).

Curtis J, Shearer G, Kohl DH. Bacteroid proline catabolism affects N2 fixation rate of drought-stressed soybeans. Plant Physiol. 136: 3313-3318 (2004).

Dallmier KA, Stewart CR. Effect of exogenous abscisic acid on proline dehydrogenase activity in maize (Zea mays L.). Plant Physiol. 99: 762-764 (1992).

de La Fuente JL, Rumbero A, Martin JF, Liras P. Delta-1-piperideine-6-carboxylate dehydrogenase, a new enzyme that forms alpha-aminoadipate in Streptomyces clavuligerus and other cephamycin C-producing actinomycetes. Biochem. J. 327: 59-64 (1997).

Deuschle K, Funck D, Forlani G, Stransky H, Biehl A, Leister D, van der Graaff E, Kunze R, Frommer WB. The role of [delta]1-pyrroline-5-carboxylate dehydrogenase in proline degradation. Plant Cell 16: 3413-3425 (2004).

Deuschle K, Funck D, Hellmann H, Daschner K, Binder S, Frommer WB. A nuclear gene encoding mitochondrial delta-pyrroline-5-carboxylate dehydrogenase and its potential role in protection from proline toxicity. Plant J. 27: 345-356 (2001).

Deutch CE. Oxidation of L-thiazolidine-4-carboxylate by L-proline dehydrogenase in Escherichia coli. J. Gen. Microbiol. 138: 1593-1598 (1992).

Deutch CE, Hasler JM, Houston RM, Sharma M, Stone VJ. Nonspecific inhibition of proline dehydrogenase synthesis in Escherichia coli during osmotic stress. Can. J. Microbiol. 35: 779-785 (1989).

Deutch CE, Klarstrom JL, Link CL, Ricciardi DL. Oxidation of L-thiazolidine-4-carboxylate by delta1-pyrroline-5-carboxylate reductase in Escherichia coli. Curr. Microbiol. 42: 442-446 (2001).

Deutch CE, O'Brien JM Jr, VanNieuwenhze MS. Identification of a trans-dominant mutation affecting proline dehydrogenase in Escherichia coli. Can. J. Microbiol. 31: 988-993 (1985).

Dluzniewska P, Gessler A, Dietrich H, Schnitzler JP, Teuber M, Rennenberg H. Nitrogen uptake and metabolism in Populus x canescens as affected by salinity. New Phytol. 173: 279-293 (2007).

Essenberg RC, Sharma YK. Cloning of genes for proline and leucine biosynthesis from Brucella abortus by functional complementation in Escherichia coli. J. Gen. Microbiol. 139: 87-93 (1993).

Flipphi M, Kocialkowska J, Felenbok B. Relationships between the ethanol utilization (alc) pathway and unrelated catabolic pathways in Aspergillus nidulans. Eur. J. Biochem. 270: 3555-3564 (2003).

Forde BG, Lea PJ. Glutamate in plants: metabolism, regulation, and signalling. J. Exp. Bot. 58: 2339-2358 (2007).

Forlani G, Mangiagalli A, Pinter C, Nielsen E. Expression of delta(1)-pyrroline-5-carboxylate dehydrogenase and proline/arginine homeostasis in Solanum tuberosum. Physiol. Plant. 110: 22-27 (2000).

Forlani G, Scainelli D, Nielsen E. Delta(1)-pyrroline-5-carboxylate dehydrogenase from cultured cells of potato: purification and properties. Plant Physiol. 113: 1413-1418 (1997).

Forlani G, Scainelli D, Nielsen E. Two delta(1)-pyrroline-5-carboxylate dehydrogenase isoforms are expressed in cultured Nicotiana plumbaginifolia cells and are differentially modulated during the culture growth cycle. Planta 202: 242-248 (1997).

Funanage VL, Ayling PD, Dendinger SM, Brenchley JE. Salmonella typhimurium LT-2 mutants with altered glutamine synthetase levels and amino acid uptake activities. J. Bacteriol. 136: 588-596 (1978).

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

Geraghty MT, Vaughn D, Nicholson AJ, Lin WW, Jimenez-Sanchez G, Obie C, Flynn MP, Valle D, Hu CA. Mutations in the delta1-pyrroline 5-carboxylate dehydrogenase gene cause type II hyperprolinemia. Hum. Mol. Genet. 7: 1411-1415 (1998).

Gogos JA, Santha M, Takacs Z, Beck KD, Luine V, Lucas LR, Nadler JV, Karayiorgou M. The gene encoding proline dehydrogenase modulates sensorimotor gating in mice. Nat. Genet. 21: 434-439 (1999).

Graham SB, Stephenson JT, Wood JM. Proline dehydrogenase from Escherichia coli K12. Reconstitution of a functional membrane association. J. Biol. Chem. 259: 2656-2661 (1984).

Grenson M. Inactivation-reactivation process and repression of permease formation regulate several ammonia-sensitive permeases in the yeast Saccharomyces cerevisiae. Eur. J. Biochem. 133: 135-139 (1983).

Hagedorn CH, Phang JM. Transfer of reducing equivalents into mitochondria by the interconversions of proline and delta 1-pyrroline-5-carboxylate. Arch. Biochem. Biophys. 225: 95-101 (1983).

Hanson J, Hanssen M, Wiese A, Hendriks MM, Smeekens S. The sucrose regulated transcription factor bZIP11 affects amino acid metabolism by regulating the expression of ASPARAGINE SYNTHETASE1 and PROLINE DEHYDROGENASE2. Plant J. 53: 935-949 (2008).

Hayashi F, Ichino T, Osanai M, Wada K. Oscillation and regulation of proline content by P5CS and ProDH gene expressions in the light/dark cycles in Arabidopsis thaliana L. Plant Cell Physiol. 41: 1096-1101 (2000).

Hayzer DJ, Leisinger T. Proline biosynthesis in Escherichia coli. Stoichiometry and end-product identification of the reaction catalysed by glutamate semialdehyde dehydrogenase. Biochem. J. 197: 269-274 (1981).

Hayzer DJ, Leisinger T. Proline biosynthesis in Escherichia coli: Purification and characterisation of glutamate-semialdehyde dehydrogenase. Eur. J. Biochem. 121: 561-565 (1982).

Hellmann H, Funck D, Rentsch D, Frommer WB. Hypersensitivity of an Arabidopsis sugar signaling mutant toward exogenous proline application. Plant Physiol. 122: 357-368 (2000).

Hellmann H, Funck D, Rentsch D, Frommer WB. Hypersensitivity of an Arabidopsis sugar signaling mutant toward exogenous proline application. Plant Physiol. 123: 779-790 (2000).

Herzfeld A, Mezl VA, Knox WE. Enzymes metabolizing delta1-pyrroline-5-carboxylate in rat tissues. Biochem. J. 166: 95-103 (1977).

Hmida-Sayari A, Gargouri-Bouzid R, Bidani A, Jaoua L, Savoure A, Jaoua S. Overexpression of Delta(1)-pyrroline-5-carboxylate synthetase increases proline production and confers salt tolerance in transgenic potato plants. Plant Sci. 169: 746-752 (2005).

Hu CA, Bart Williams D, Zhaorigetu S, Khalil S, Wan G, Valle D. Functional genomics and SNP analysis of human genes encoding proline metabolic enzymes. Amino Acids 35: 655-664 (2008).

Hu CA, Delauney AJ, Verma DP. A bifunctional enzyme (delta 1-pyrroline-5-carboxylate synthetase) catalyzes the first two steps in proline biosynthesis in plants. Proc. Natl. Acad. Sci. U.S.A. 89: 9354-9358 (1992).

Hu CA, Lin WW, Valle D. Cloning, characterization, and expression of cDNAs encoding human delta 1-pyrroline-5-carboxylate dehydrogenase. J. Biol. Chem. 271: 9795-9800 (1996).

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).

Huang TC, Huang YW, Hung HJ, Ho CT, Wu ML. Delta1-pyrroline-5-carboxylic acid formed by proline dehydrogenase from the Bacillus subtilis ssp natto expressed in Escherichia coli as a precursor for 2-acetyl-1-pyrroline. J. Agric. Food Chem. 55: 5097-5102 (2007).

Humbertclaude V, Rivier F, Roubertie A, Echenne B, Bellet H, Vallat C, Morin D. Is hyperprolinemia type I actually a benign trait? Report of a case with severe neurologic involvement and vigabatrin intolerance. J. Child Neurol. 16: 622-623 (2001).

Hurry V, Strand A, Furbank R, Stitt M. The role of inorganic phosphate in the development of freezing tolerance and the acclimatization of photosynthesis to low temperature is revealed by the pho mutants of Arabidopsis thaliana. Plant J. 24: 383-396 (2000).

Igarashi Y, Yoshiba Y, Takeshita T, Nomura S, Otomo J, Yamaguchi-Shinozaki K, Shinozaki K. Molecular cloning and characterization of a cDNA encoding proline transporter in rice. Plant Cell Physiol. 41: 750-756 (2000).

Jimenez-Zurdo JI, Garcia-Rodriguez FM, Toro N. The Rhizobium meliloti putA gene: its role in the establishment of the symbiotic interaction with alfalfa. Mol. Microbiol. 23: 85-93 (1997).

Jimenez-Zurdo JI, van Dillewijn P, Soto MJ, de Felipe MR, Olivares J, Toro N. Characterization of a Rhizobium meliloti proline dehydrogenase mutant altered in nodulation efficiency and competitiveness on alfalfa roots. Mol. Plant Microbe Interact. 8: 492-498 (1995).

Kamiya A, Inoue Y, Kodama T, Gonzalez FJ. Hepatocyte nuclear factors 1alpha and 4alpha control expression of proline oxidase in adult liver. FEBS Lett. 578: 63-68 (2004).

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Keuntje B, Masepohl B, Klipp W. Expression of the putA gene encoding proline dehydrogenase from Rhodobacter capsulatus is independent of NtrC regulation but requires an Lrp-like activator protein. J. Bacteriol. 177: 6432-6439 (1995).

Kiyosue T, Yoshiba Y, Yamaguchi-Shinozaki K, Shinozaki K. A nuclear gene encoding mitochondrial proline dehydrogenase, an enzyme involved in proline metabolism, is upregulated by proline but downregulated by dehydration in Arabidopsis. Plant Cell 8: 1323-1335 (1996).

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Krishnan N, Dickman MB, Becker DF. Proline modulates the intracellular redox environment and protects mammalian cells against oxidative stress. Free Radic. Biol. Med. 44: 671-681 (2008).

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Lin JW, Yu KY, Chen HY, Weng SF. Regulatory region with putA gene of proline dehydrogenase that links to the lum and the lux operons in Photobacterium leiognathi. Biochem. Biophys. Res. Commun. 219: 868-875 (1996).

Ling M, Allen SW, Wood JM. Sequence analysis identifies the proline dehydrogenase and delta 1-pyrroline-5-carboxylate dehydrogenase domains of the multifunctional Escherichia coli PutA protein. J. Mol. Biol. 243: 950-956 (1994).

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Manfre F, Kern J-M, Biellmann J-F. Synthesis of proline analogues as potential mechanism-based inhibitors of proline dehydrogenase: 4-methylene-L-, (E)- and (Z)-4-(fluromethylene)-L-. cis and trans-5-ethynyl-(+/-)-, and cis- and trans-5-vinyl-L-proline. J. Org. Chem. 57: 2060-2065 (1992).

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Menzel R, Roth J. Purification of the putA gene product. A bifunctional membrane-bound protein from Salmonella typhimurium responsible for the two-step oxidation of proline to glutamate. J. Biol. Chem. 256: 9755-9761 (1981).

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Ratzkin B, Roth J. Cluster of genes controlling proline degradation in Salmonella typhimurium. J. Bacteriol. 133: 744-754 (1978).

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Sakuraba H, Takamatsu Y, Satomura T, Kawakami R, Ohshima T. Purification, characterization, and application of a novel dye- linked L-proline dehydrogenase from a hyperthermophilic archaeon, Thermococcus profundus. Appl. Environ. Microbiol. 67: 1470-1475 (2001).

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