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Journal articles on the topic 'Pyrroline-5-carboxylate'

Author: Grafiati

Published: 25 May 2024

Last updated: 31 July 2025

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1

Merrill, M. J., G. C. Yeh, and J. M. Phang. "Purified Human Erythrocyte Pyrroline-5-carboxylate Reductase." Journal of Biological Chemistry 264, no. 16 (1989): 9352–58. http://dx.doi.org/10.1016/s0021-9258(18)60538-1.

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2

Zhao, Man, Linlin Qian, Zhuoyu Chi, et al. "Combined Metabolomic and Quantitative RT-PCR Analyses Revealed the Synthetic Differences of 2-Acetyl-1-pyrroline in Aromatic and Non-Aromatic Vegetable Soybeans." International Journal of Molecular Sciences 23, no. 23 (2022): 14529. http://dx.doi.org/10.3390/ijms232314529.

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Aroma is an important economic trait of vegetable soybeans, which greatly influences their market value. The 2-acetyl-1-pyrroline (2AP) is considered as an important substance affecting the aroma of plants. Although the 2AP synthesis pathway has been resolved, the differences of the 2AP synthesis in the aromatic and non-aromatic vegetable soybeans are unknown. In this study, a broad targeted metabolome analysis including measurement of metabolites levels and gene expression levels was performed to reveal pathways of aroma formation in the two developmental stages of vegetable soybean grains [3

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3

Vettore, Lisa, Rebecca Westbrook, Jennie Roberts, et al. "FSMP-12. A ROLE FOR PROLINE BIOSYNTHESIS IN HYPOXIC GLIOBLASTOMA." Neuro-Oncology Advances 3, Supplement_1 (2021): i18. http://dx.doi.org/10.1093/noajnl/vdab024.076.

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Abstract Hypoxia is a common feature of glioblastoma, and a known driver of therapy resistance in brain tumours. Understanding the metabolic adaptations to hypoxia is key to develop new effective treatments for patients. A recent screening study highlighted Pyrroline-5-carboxylate reductase-like (PYCRL) as one of the top three genes that allowed tumour survival in hypoxia. PYCRL is one of the three enzymes involved in proline biosynthesis along with the mitochondrial pyrroline-5-carboxylate reductase 1 and 2 (PYCR1/2). The latter use glutamine as the carbon source to fuel the pyrroline-5-carbo

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4

Meng, Zhaohui, Zhiyong Lou, Zhe Liu, et al. "Crystal Structure of Human Pyrroline-5-carboxylate Reductase." Journal of Molecular Biology 359, no. 5 (2006): 1364–77. http://dx.doi.org/10.1016/j.jmb.2006.04.053.

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5

Wu, G., D. A. Knabe, and N. E. Flynn. "Synthesis of citrulline from glutamine in pig enterocytes." Biochemical Journal 299, no. 1 (1994): 115–21. http://dx.doi.org/10.1042/bj2990115.

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The synthesis of citrulline from glutamine was quantified in enterocytes from pre-weaning (14-21 days old) and post-weaning (29-58 days old) pigs. The cells were incubated at 37 degrees C for 30 min in Krebs-Henseleit bicarbonate buffer (pH 7.4) containing 0, 0.5, 2 and 5 mM glutamine. Oxygen consumption was linear during the 30 min incubation period. The rates of citrulline synthesis were low or negligible in enterocytes from 14-21-day-old pigs, but increased 10-20-fold in the cells from 29-58-day-old pigs. This marked elevation of citrulline synthesis coincided with an increase in the activi

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6

Hu, C. A. A., S. Khalil, S. Zhaorigetu та ін. "Human Δ1-pyrroline-5-carboxylate synthase: function and regulation". Amino Acids 35, № 4 (2008): 665–72. http://dx.doi.org/10.1007/s00726-008-0075-0.

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7

Hu, Chien-an A., Wei-Wen Lin, Cassandra Obie та David Valle. "Molecular Enzymology of Mammalian Δ1-Pyrroline-5-carboxylate Synthase". Journal of Biological Chemistry 274, № 10 (1999): 6754–62. http://dx.doi.org/10.1074/jbc.274.10.6754.

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8

Small, Curtis, and Mary Ellen Jones. "A specific radiochemical assay for pyrroline-5-carboxylate dehydrogenase." Analytical Biochemistry 161, no. 2 (1987): 380–86. http://dx.doi.org/10.1016/0003-2697(87)90466-0.

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9

Basch, J. J., E. D. Wickham, and H. M. Farrell. "Pyrroline-5-Carboxylate Reductase in Lactating Bovine Mammary Glands." Journal of Dairy Science 79, no. 8 (1996): 1361–68. http://dx.doi.org/10.3168/jds.s0022-0302(96)76493-7.

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10

Farrés, J., P. Julià, and X. Parés. "Aldehyde oxidation in human placenta. Purification and properties of 1-pyrroline-5-carboxylate dehydrogenase." Biochemical Journal 256, no. 2 (1988): 461–67. http://dx.doi.org/10.1042/bj2560461.

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The human placenta contains a considerable amount of 1-pyrroline-5-carboxylate dehydrogenase (23 +/- 6 micrograms/g; n = 12), about 25% of the concentration present in liver. The enzyme is the only form in placenta that oxidizes short- and medium-chain aldehydes, which facilitates its purification from this organ. It can be purified to homogeneity by successive chromatographies on DEAE-cellulose, 5′-AMP-Sepharose and Sephacryl S-300. From 500 g of tissue, about 2.1 units of enzyme can be obtained with a 12% yield. Placental 1-pyrroline-5-carboxylate dehydrogenase is a dimer of Mr-63,000 subuni

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11

Luo, Qiaoyu, Yonggui Ma, Huichun Xie, et al. "Proline Metabolism in Response to Climate Extremes in Hairgrass." Plants 13, no. 10 (2024): 1408. http://dx.doi.org/10.3390/plants13101408.

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Hairgrass (Deschampsia caespitosa), a widely distributed grass species considered promising in the ecological restoration of degraded grassland in the Qinghai-Xizang Plateau, is likely to be subjected to frequent drought and waterlogging stress due to ongoing climate change, further aggravating the degradation of grassland in this region. However, whether it would acclimate to water stresses resulting from extreme climates remains unknown. Proline accumulation is a crucial metabolic response of plants to challenging environmental conditions. This study aims to investigate the changes in prolin

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12

Krueger, Rolf, Hans-Jürgen Jäger, Martin Hintz, and Edwin Pahlich. "Purification to Homogeneity of Pyrroline-5-Carboxylate Reductase of Barley." Plant Physiology 80, no. 1 (1986): 142–44. http://dx.doi.org/10.1104/pp.80.1.142.

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13

Meng, Zhaohui, Zhiyong Lou, Zhe Liu, Dong Hui, Mark Bartlam, and Zihe Rao. "Purification, characterization, and crystallization of human pyrroline-5-carboxylate reductase." Protein Expression and Purification 49, no. 1 (2006): 83–87. http://dx.doi.org/10.1016/j.pep.2006.02.019.

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14

Inagaki, Eiji, Noriyasu Ohshima, Hitomi Takahashi, Chizu Kuroishi, Shigeyuki Yokoyama та TahirH Tahirov. "Crystal Structure of Thermus thermophilus Δ1-Pyrroline-5-carboxylate Dehydrogenase". Journal of Molecular Biology 362, № 3 (2006): 490–501. http://dx.doi.org/10.1016/j.jmb.2006.07.048.

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15

Shiono, Takashi, Peter F. Kador, and Jin J. Kinoshita. "Purification and characterization of rat lens pyrroline-5-carboxylate reductase." Biochimica et Biophysica Acta (BBA) - General Subjects 881, no. 1 (1986): 72–78. http://dx.doi.org/10.1016/0304-4165(86)90098-x.

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16

Fahmy, Afaf S., Saleh A. Mohamed, Rasmy B. Girgis та Fathy A. Abdel-Ghaffar. "Enzymes of Δ1-Pyrroline-5-Carboxylate Metabolism in the Camel Tick Hyalomma dromedarii During Embryogenesis. Purification and Characterization of Δ1-Pyrroline-5-Carboxylate Dehydrogenases". Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 118, № 1 (1997): 229–37. http://dx.doi.org/10.1016/s0305-0491(97)00053-9.

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17

de la FUENTE, Juan L., Angel RUMBERO, Juan F. MARTÍN та Paloma LIRAS. "Δ-1-Piperideine-6-carboxylate dehydrogenase, a new enzyme that forms α-aminoadipate in Streptomyces clavuligerus and other cephamycin C-producing actinomycetes". Biochemical Journal 327, № 1 (1997): 59–64. http://dx.doi.org/10.1042/bj3270059.

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Δ-1-Piperideine-6-carboxylate (P6C) dehydrogenase activity, which catalyses the conversion of P6C into α-aminoadipic acid, has been studied in the cephamycin C producer Streptomyces clavuligerus by both spectrophotometric and radiometric assays. The enzyme has been purified 124-fold to electrophoretic homogeneity with a 26% yield. The native protein is a monomer of 56.2 kDa that efficiently uses P6C (apparent Km 14 μM) and NAD+ (apparent Km 115 μM), but not NADP+ or other electron acceptors, as substrates. The enzyme activity was inhibited (by 66%) by its end product NADH at 0.1 mM concentrati

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18

Terao, Yukiyasu, Shigeru Nakamori, and Hiroshi Takagi. "Gene Dosage Effect of l-Proline Biosynthetic Enzymes on l-Proline Accumulation and Freeze Tolerance in Saccharomyces cerevisiae." Applied and Environmental Microbiology 69, no. 11 (2003): 6527–32. http://dx.doi.org/10.1128/aem.69.11.6527-6532.2003.

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ABSTRACT We have previously reported that l-proline has cryoprotective activity in Saccharomyces cerevisiae. A freeze-tolerant mutant with l-proline accumulation was recently shown to carry an allele of the PRO1 gene encoding γ-glutamyl kinase, which resulted in a single amino acid substitution (Asp154Asn). Interestingly, this mutation enhanced the activities of γ-glutamyl kinase and γ-glutamyl phosphate reductase, both of which catalyze the first two steps of l-proline synthesis and which together may form a complex in vivo. Here, we found that the Asp154Asn mutant γ-glutamyl kinase was more

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19

Biancalana, Lorenzo, Giada Tuci, Fabio Piccinelli, Fabio Marchetti, Marco Bortoluzzi, and Guido Pampaloni. "Vanadium(v) oxoanions in basic water solution: a simple oxidative system for the one pot selective conversion ofl-proline to pyrroline-2-carboxylate." Dalton Transactions 46, no. 43 (2017): 15059–69. http://dx.doi.org/10.1039/c7dt02702h.

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The unusual, one pot conversion ofl-proline to pyrroline-2-carboxylate, using simple V(v) species (NH<sub>4</sub>VO<sub>3</sub>or V<sub>2</sub>O<sub>5</sub>) as oxidants in basic water medium, is described. No reaction was observed with primary and tertiary α-amino acids.

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20

Deutch, Charles E., Jessica L. Klarstrom, Casey L. Link та Dominic L. Ricciardi. "Oxidation of l-Thiazolidine-4-Carboxylate by Δ1-Pyrroline-5-Carboxylate Reductase in Escherichia coli". Current Microbiology 42, № 6 (2001): 442–46. http://dx.doi.org/10.1007/s002840010245.

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21

Ishikawa, Hiroaki, Takeo Matsuzawa, Koji Ohashi, and Yoichi Nagamura. "A novel method for measuring serum ornithine carbamoyltransferase." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 40, no. 3 (2003): 264–68. http://dx.doi.org/10.1258/000456303321610583.

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Background: Serum ornithine carbamoyltransferase is a diagnostic marker of hepatic disorders due to its localization in periportal mitochondria. Methods: We have developed a new method for the determination of serum ornithine carbamoyltransferase. It is based on the reverse reaction of ornithine carbamoyltransferase, using ornithine-ketoacid aminotransferase, ∆1-pyrroline-5-carboxylate dehydrogenase and glutamate dehydrogenase, which together convert citrulline through ornithine to glutamate. The glutamate is then quantitatively measured using glutamate oxidase and Trinder's reagent. Results:

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22

Patel, Sagar M., Javier Seravalli, Xinwen Liang, John J. Tanner та Donald F. Becker. "Disease variants of human Δ1-pyrroline-5-carboxylate reductase 2 (PYCR2)". Archives of Biochemistry and Biophysics 703 (травень 2021): 108852. http://dx.doi.org/10.1016/j.abb.2021.108852.

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23

Patel, Sagar M., Javier Seravalli, Kyle M. Stiers, John J. Tanner, and Donald F. Becker. "Kinetics of human pyrroline-5-carboxylate reductase in l-thioproline metabolism." Amino Acids 53, no. 12 (2021): 1863–74. http://dx.doi.org/10.1007/s00726-021-03095-4.

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24

Isobe, Kimiyasu, Takeo Matsuzawa, and Kenji Soda. "Crystallization and Characterization of l-Pyrroline-5-carboxylate Dehydrogenase fromBacillus sphaericus." Agricultural and Biological Chemistry 51, no. 7 (1987): 1947–53. http://dx.doi.org/10.1080/00021369.1987.10868323.

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25

Hua, X. J., B. van de Cotte, M. Van Montagu, and N. Verbruggen. "Developmental Regulation of Pyrroline-5-Carboxylate Reductase Gene Expression in Arabidopsis." Plant Physiology 114, no. 4 (1997): 1215–24. http://dx.doi.org/10.1104/pp.114.4.1215.

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26

Deuschle, Karen, Dietmar Funck, Giuseppe Forlani та ін. "The Role of Δ1-Pyrroline-5-Carboxylate Dehydrogenase in Proline Degradation". Plant Cell 16, № 12 (2004): 3413–25. http://dx.doi.org/10.1105/tpc.104.023622.

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27

FLEMING, G. A., A. GRANGER, Q. R. ROGERS, M. PROSSER, D. B. FORD, and J. M. PHANG. "Fluctuations in Plasma Pyrroline-5-Carboxylate Concentrations during Feeding and Fasting*." Journal of Clinical Endocrinology & Metabolism 69, no. 2 (1989): 448–52. http://dx.doi.org/10.1210/jcem-69-2-448.

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28

Black, David StC, Gavin L. Edwards, Richard H. Evans, Paul A. Keller, and Sean M. Laaman. "Synthesis and Reactivity of 1-Pyrroline-5-carboxylate Ester 1-Oxides." Tetrahedron 56, no. 13 (2000): 1889–97. http://dx.doi.org/10.1016/s0040-4020(00)00094-6.

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29

Wong, P. T. H., W. L. Teo та S. F. Leong. "Some characteristics of Δ1-pyrroline-5-carboxylate dehydrogenase in rat cerebellum". Neurochemistry International 7, № 1 (1985): 45–49. http://dx.doi.org/10.1016/0197-0186(85)90006-3.

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30

Verbruggen, N., R. Villarroel, and M. Van Montagu. "Osmoregulation of a Pyrroline-5-Carboxylate Reductase Gene in Arabidopsis thaliana." Plant Physiology 103, no. 3 (1993): 771–81. http://dx.doi.org/10.1104/pp.103.3.771.

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31

Krause, Kurt L., Emily M. Christensen, Sagar M. Patel, et al. "Correcting the record – cofactor binding of human pyrroline-5-carboxylate reductase." Acta Crystallographica Section A Foundations and Advances 73, a2 (2017): C49. http://dx.doi.org/10.1107/s2053273317095213.

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32

Christensen, Emily M., Alexandra N. Bogner, Anke Vandekeere, et al. "In crystallo screening for proline analog inhibitors of the proline cycle enzyme PYCR1." Journal of Biological Chemistry 295, no. 52 (2020): 18316–27. http://dx.doi.org/10.1074/jbc.ra120.016106.

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Pyrroline-5-carboxylate reductase 1 (PYCR1) catalyzes the biosynthetic half-reaction of the proline cycle by reducing Δ1-pyrroline-5-carboxylate (P5C) to proline through the oxidation of NAD(P)H. Many cancers alter their proline metabolism by up-regulating the proline cycle and proline biosynthesis, and knockdowns of PYCR1 lead to decreased cell proliferation. Thus, evidence is growing for PYCR1 as a potential cancer therapy target. Inhibitors of cancer targets are useful as chemical probes for studying cancer mechanisms and starting compounds for drug discovery; however, there is a notable la

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33

Struys, Eduard A., Erwin E. W. Jansen та Gajja S. Salomons. "Human pyrroline-5-carboxylate reductase (PYCR1) acts on Δ1-piperideine-6-carboxylate generating L-pipecolic acid". Journal of Inherited Metabolic Disease 37, № 3 (2014): 327–32. http://dx.doi.org/10.1007/s10545-013-9673-4.

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34

Belitsky, Boris R., Jeanette Brill, Erhard Bremer, and Abraham L. Sonenshein. "Multiple Genes for the Last Step of Proline Biosynthesis in Bacillus subtilis." Journal of Bacteriology 183, no. 14 (2001): 4389–92. http://dx.doi.org/10.1128/jb.183.14.4389-4392.2001.

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ABSTRACT The complete Bacillus subtilis genome contains four genes (proG, proH, proI, and comER) with the potential to encode Δ1-pyrroline-5-carboxylate reductase, a proline biosynthetic enzyme. Simultaneous defects in three of these genes (proG, proH, and proI) were required to confer proline auxotrophy, indicating that the products of these genes are mostly interchangeable with respect to the last step in proline biosynthesis.

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35

Hu, Chien-an A., Wei-Wen Lin, and David Valle. "Cloning, Characterization, and Expression of cDNAs Encoding Human -Pyrroline-5-carboxylate Dehydrogenase." Journal of Biological Chemistry 271, no. 16 (1996): 9795–800. http://dx.doi.org/10.1074/jbc.271.16.9795.

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36

Mixson, A. James, Alnora N. Granger, and James M. Phang. "An Assay for Pyrroline 5-Carboxylate Based on its Interaction with Cysteine." Analytical Letters 24, no. 4 (1991): 625–41. http://dx.doi.org/10.1080/00032719108052931.

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37

ISOBE, Kimiyasu, Takeo MATSUZAWA, and Kenji SODA. "Crystallization and characterization of 1-pyrroline-5-carboxylate dehydrogenase from Bacillus sphaericus." Agricultural and Biological Chemistry 51, no. 7 (1987): 1947–53. http://dx.doi.org/10.1271/bbb1961.51.1947.

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38

Rayapati, P. John, Cecil R. Stewart, and Ethan Hack. "Pyrroline-5-Carboxylate Reductase Is in Pea (Pisum sativum L.) Leaf Chloroplasts." Plant Physiology 91, no. 2 (1989): 581–86. http://dx.doi.org/10.1104/pp.91.2.581.

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39

Dougherty, K. M., M. C. Brandriss, and D. Valle. "Cloning human pyrroline-5-carboxylate reductase cDNA by complementation in Saccharomyces cerevisiae." Journal of Biological Chemistry 267, no. 2 (1992): 871–75. http://dx.doi.org/10.1016/s0021-9258(18)48364-0.

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40

Mixson, A. James, and James M. Phang. "Structural analogues of pyrroline 5-carboxylate specifically inhibit its uptake into cells." Journal of Membrane Biology 121, no. 3 (1991): 269–77. http://dx.doi.org/10.1007/bf01951560.

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41

Haslett, Michael R., Desmond Pink, Barry Walters, and Margaret E. Brosnan. "Assay and subcellular localization of pyrroline-5-carboxylate dehydrogenase in rat liver." Biochimica et Biophysica Acta (BBA) - General Subjects 1675, no. 1-3 (2004): 81–86. http://dx.doi.org/10.1016/j.bbagen.2004.08.008.

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42

Fleming, G. Alexander, Gary Steel, David Valle, Alnora S. Granger, and James M. Phang. "The aqueous humor of rabbit contains high concentrations of pyrroline-5-carboxylate." Metabolism 35, no. 10 (1986): 933–37. http://dx.doi.org/10.1016/0026-0495(86)90057-0.

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43

Samuels, Susan E., Karen S. Acton, and Ronald O. Ball. "Pyrroline-5-Carboxylate Reductase and Proline Oxidase Activity in the Neonatal Pig." Journal of Nutrition 119, no. 12 (1989): 1999–2004. http://dx.doi.org/10.1093/jn/119.12.1999.

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44

Trakadis, Y., A. Khan, C. Ste Martin, M. Berry, and D. Buhas. "Two new unrelated cases of pyrroline-5-carboxylate synthase — New founder effect?" Clinical Biochemistry 47, no. 15 (2014): 145. http://dx.doi.org/10.1016/j.clinbiochem.2014.07.061.

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45

Giberti, Samuele, Michele Bertazzini, Mattia Liboni, Łukasz Berlicki, Paweł Kafarski та Giuseppe Forlani. "Phytotoxicity of aminobisphosphonates targeting bothδ1-pyrroline-5-carboxylate reductase and glutamine synthetase". Pest Management Science 73, № 2 (2016): 435–43. http://dx.doi.org/10.1002/ps.4299.

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46

ZHANG, Fei, Jia-Dong HE, Qiu-Dan NI, Qiang-Sheng WU, and Ying-Ning ZOU. "Enhancement of Drought Tolerance in Trifoliate Orange by Mycorrhiza: Changes in Root Sucrose and Proline Metabolisms." Notulae Botanicae Horti Agrobotanici Cluj-Napoca 46, no. 1 (2018): 270–76. http://dx.doi.org/10.15835/nbha46110983.

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Sucrose and proline metabolisms are often associated with drought tolerance of plants. This study was conducted to investigate the effects of two arbuscular mycorrhizal fungi (AMF) species (Funneliformis mosseae and Paraglomus occultum) on root biomass, lateral root number, root sucrose and proline metabolisms in trifoliate orange (Poncirus trifoliata) seedlings under well-watered (WW) or drought stress (DS). All the AMF treatments significantly increased root dry weight, taproot length, and the number of lateral roots in 1st, 2nd, and 3rd class under WW and DS. Mycorrhizal seedlings conferred

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47

Katerova, Zornitsa, Dessislava Todorova, Irina I. Vaseva, et al. "Effects of Melatonin Pre- and Post-Drought Treatment on Oxidative Stress Markers and Expression of Proline-Related Transcripts in Young Wheat Plants." International Journal of Molecular Sciences 25, no. 22 (2024): 12127. http://dx.doi.org/10.3390/ijms252212127.

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Wheat can tolerate a mild water deficit, but prolonged drought causes a number of detrimental physiological changes resulting in a substantial decrease in productivity. The present study evaluates the potential of the natural plant growth regulator melatonin to alleviate the negative effects of moderate drought in two Bulgarian winter wheat cultivars at the early vegetative stage. Melatonin doses of 75 µM were root-supplemented 24 h before or after the stress period. The levels of several biometric parameters, osmolyte content and stress indicators as well as the expression of genes coding for

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48

Li, Linhua, Yujia Ye, Peng Sang, et al. "Effect of R119G Mutation on Human P5CR1 Dynamic Property and Enzymatic Activity." BioMed Research International 2017 (2017): 1–8. http://dx.doi.org/10.1155/2017/4184106.

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Pyrroline-5-carboxylate reductase (P5CR1) is a universal housekeeping enzyme that catalyzes the reduction of Δ1-pyrroline-5-carboxylate (P5C) to proline with concomitant oxidation of NAD(P)H to NAD(P)+. The enzymatic cycle between P5C and proline is important for function in amino acid metabolism, apoptosis, and intracellular redox potential balance in mitochondria. Autosomal recessive cutis laxa (ARCL) results from a mutation in P5CR1 encoded by PYCR1. Specifically, the R119G mutation is reported to be linked to ARCL although it has not yet been characterized. We synthesized R119G P5CR1 and c

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49

Dong, Shupeng, Zhuozhuo Mao, Zhongyi Yang, et al. "A Soybean Pyrroline-5-Carboxylate Dehydrogenase GmP5CDH1 Modulates Plant Growth and Proline Sensitivity." Agronomy 14, no. 10 (2024): 2411. http://dx.doi.org/10.3390/agronomy14102411.

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Soybean [Glycine max (L.) Merr.], as a globally commercialized crop, is an important source of protein and oil for both humans and livestock. With more frequent extreme weather disasters, abiotic stress has become one of the critical factors restricting soybean production. Proline (Pro) is a well-known substance in plants that responds to abiotic stress. To identify potential effector genes involved in soybean resistance to abiotic stress, we focused on the pyrroline-5-carboxylate dehydrogenase (P5CDH) which is a key enzyme in the degradation process of Pro. Through homologous sequence alignme

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50

Razavizadeh, Roya, and Ali Ehsanpour. "Effects of salt stress on proline content, expression of delta-1-pyrroline-5-carboxylate synthetase, and activities of catalase and ascorbate peroxidase in transgenic tobacco plants." Biological Letters 46, no. 2 (2009): 63–75. http://dx.doi.org/10.2478/v10120-009-0002-4.

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Effects of salt stress on proline content, expression of delta-1-pyrroline-5-carboxylate synthetase, and activities of catalase and ascorbate peroxidase in transgenic tobacco plantsIn arid and semiarid regions, soil salinity limits crop production. Proline accumulation in transgenic plants results in increased stress tolerance, but the underlying mechanism was unclear. To elucidate it, effects of salt stress on the expression pattern of Δ1-pyrroline-5-carboxylate synthetase (P5CS), proline content, catalase (CAT), and ascorbate peroxidase (APX) activities were analyzed in transgenic tobacco (N

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