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Relevant bibliographies by topics / Pyrroline-5-carboxylate complex

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Academic literature on the topic 'Pyrroline-5-carboxylate complex'

Author: Grafiati

Published: 25 May 2024

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Journal articles on the topic "Pyrroline-5-carboxylate complex"

1

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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2

Ion, Bogdan F., Mohamed M. Aboelnga та James W. Gauld. "Insights from molecular dynamics on substrate binding and effects of active site mutations in Δ1-pyrroline-5-carboxylate dehydrogenase". Canadian Journal of Chemistry 94, № 12 (2016): 1151–62. http://dx.doi.org/10.1139/cjc-2016-0286.

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The NAD+-dependent enzyme, Δ1-pyrroline-5-carboxylate dehydrogenase (P5CDH), has an important role in proline and hydroxyproline catabolism for humans. Specifically, this aldehyde dehydrogenase is responsible for the oxidation of both l-glutamate-γ-semialdehyde (GSA) and 4-erythro-hydroxy-l-glutamate-γ-semialdehyde (4-OH-GSA) to their respective l-glutamate product forms. We have performed a detailed molecular dynamics (MD) study of both the reactant and product complex structures of P5CDH to gain insights into ligand binding (i.e., GSA, 4-OH-GSA, NAD+, GLU) in the active site. Moreover, our i

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3

Kretz, Rita, Bita Bozorgmehr, Mohamad Hasan Kariminejad, et al. "Defect in proline synthesis: pyrroline-5-carboxylate reductase 1 deficiency leads to a complex clinical phenotype with collagen and elastin abnormalities." Journal of Inherited Metabolic Disease 34, no. 3 (2011): 731–39. http://dx.doi.org/10.1007/s10545-011-9319-3.

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4

Pallag, Gergely, Sara Nazarian, Dora Ravasz, et al. "Proline Oxidation Supports Mitochondrial ATP Production When Complex I Is Inhibited." International Journal of Molecular Sciences 23, no. 9 (2022): 5111. http://dx.doi.org/10.3390/ijms23095111.

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The oxidation of proline to pyrroline-5-carboxylate (P5C) leads to the transfer of electrons to ubiquinone in mitochondria that express proline dehydrogenase (ProDH). This electron transfer supports Complexes CIII and CIV, thus generating the protonmotive force. Further catabolism of P5C forms glutamate, which fuels the citric acid cycle that yields the reducing equivalents that sustain oxidative phosphorylation. However, P5C and glutamate catabolism depend on CI activity due to NAD+ requirements. NextGen-O2k (Oroboros Instruments) was used to measure proline oxidation in isolated mitochondria

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5

Silao, Fitz Gerald S., Tong Jiang, Biborka Bereczky-Veress, et al. "Proline catabolism is a key factor facilitating Candida albicans pathogenicity." PLOS Pathogens 19, no. 11 (2023): e1011677. http://dx.doi.org/10.1371/journal.ppat.1011677.

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Candida albicans, the primary etiology of human mycoses, is well-adapted to catabolize proline to obtain energy to initiate morphological switching (yeast to hyphal) and for growth. We report that put1-/- and put2-/- strains, carrying defective Proline UTilization genes, display remarkable proline sensitivity with put2-/- mutants being hypersensitive due to the accumulation of the toxic intermediate pyrroline-5-carboxylate (P5C), which inhibits mitochondrial respiration. The put1-/- and put2-/- mutations attenuate virulence in Drosophila and murine candidemia models and decrease survival in hu

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6

Lagautriere, Thomas, Ghader Bashiri та Edward N. Baker. "Use of a “silver bullet” to resolve crystal lattice dislocation disorder: A cobalamin complex of Δ1-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis". Journal of Structural Biology 189, № 2 (2015): 153–57. http://dx.doi.org/10.1016/j.jsb.2014.12.007.

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7

Sun, Chenglong, Tiegang Li, Xiaowei Song, et al. "Spatially resolved metabolomics to discover tumor-associated metabolic alterations." Proceedings of the National Academy of Sciences 116, no. 1 (2018): 52–57. http://dx.doi.org/10.1073/pnas.1808950116.

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Characterization of tumor metabolism with spatial information contributes to our understanding of complex cancer metabolic reprogramming, facilitating the discovery of potential metabolic vulnerabilities that might be targeted for tumor therapy. However, given the metabolic variability and flexibility of tumors, it is still challenging to characterize global metabolic alterations in heterogeneous cancer. Here, we propose a spatially resolved metabolomics approach to discover tumor-associated metabolites and metabolic enzymes directly in their native state. A variety of metabolites localized in

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8

Yildiz, Ibrahim. "Computational insights on the hydride and proton transfer mechanisms of L-proline dehydrogenase." PLOS ONE 18, no. 11 (2023): e0290901. http://dx.doi.org/10.1371/journal.pone.0290901.

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L-Proline dehydrogenase (ProDH) is a flavin-dependent oxidoreductase, which catalyzes the oxidation of L-proline to (S)-1-pyrroline-5-carboxylate. Based on the experimental studies, a stepwise proton and hydride transfer mechanism is supported. According to this mechanism, the amino group of L-proline is deprotonated by a nearby Lys residue, which is followed by the hydride transfer process from C5 position of L-proline to N5 position of isoalloxazine ring of FAD. It was concluded that the hydride transfer step is rate limiting in the reductive half-reaction, however, in the overall reaction,

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9

DelVecchio, Vito G., Joseph P. Connolly, Timothy G. Alefantis, et al. "Proteomic Profiling and Identification of Immunodominant Spore Antigens of Bacillus anthracis, Bacillus cereus, and Bacillus thuringiensis." Applied and Environmental Microbiology 72, no. 9 (2006): 6355–63. http://dx.doi.org/10.1128/aem.00455-06.

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ABSTRACT Differentially expressed and immunogenic spore proteins of the Bacillus cereus group of bacteria, which includes Bacillus anthracis, Bacillus cereus, and Bacillus thuringiensis, were identified. Comparative proteomic profiling of their spore proteins distinguished the three species from each other as well as the virulent from the avirulent strains. A total of 458 proteins encoded by 232 open reading frames were identified by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry analysis for all the species. A number of highly expressed proteins, including elonga

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10

Lewoniewska, Sylwia, Ilona Oscilowska, Antonella Forlino, and Jerzy Palka. "Understanding the Role of Estrogen Receptor Status in PRODH/POX-Dependent Apoptosis/Survival in Breast Cancer Cells." Biology 10, no. 12 (2021): 1314. http://dx.doi.org/10.3390/biology10121314.

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It has been suggested that activation of estrogen receptor α (ER α) stimulates cell proliferation. In contrast, estrogen receptor β (ER β) has anti-proliferative and pro-apoptotic activity. Although the role of estrogens in estrogen receptor-positive breast cancer progression has been well established, the mechanism of their effect on apoptosis is not fully understood. It has been considered that ER status of breast cancer cells and estrogen availability might determine proline dehydrogenase/proline oxidase (PRODH/POX)-dependent apoptosis. PRODH/POX is a mitochondrial enzyme that converts prol

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