Relevant bibliographies by topics / Ribulose-5-phosphate-3-epimerase

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Academic literature on the topic 'Ribulose-5-phosphate-3-epimerase'

Author: Grafiati
Published: 7 June 2025
Last updated: 16 July 2025

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Journal articles on the topic "Ribulose-5-phosphate-3-epimerase"

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Meloni, Maria, Silvia Fanti, Daniele Tedesco, et al. "Characterization of chloroplast ribulose-5-phosphate-3-epimerase from the microalga Chlamydomonas reinhardtii." Plant Physiology 194, no. 4 (2023): 2263–77. https://doi.org/10.1093/plphys/kiad680.

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<em>This is a pre-copyedited, author-produced version of an article accepted for publication in Plant Physiology following peer review. The version of record [Maria Meloni, Silvia Fanti, Daniele Tedesco, Libero Gurrieri, Paolo Trost, Simona Fermani, St&eacute;phane D. Lemaire, Mirko Zaffagnini, Julien Henri, Characterization of chloroplast ribulose-5-phosphate-3-epimerase from the microalga Chlamydomonas reinhardtii, Plant Physiology, Volume 194, Issue 4, April 2024, Pages 2263&ndash;2277] is available online at: https://academic.oup.com/plphys/article/194/4/2263/7491446 [DOI: 10.1093/plphys/k
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Yew, Wen Shan, and John A. Gerlt. "Utilization of l-Ascorbate by Escherichia coli K-12: Assignments of Functions to Products of the yjf-sga and yia-sgb Operons." Journal of Bacteriology 184, no. 1 (2002): 302–6. http://dx.doi.org/10.1128/jb.184.1.302-306.2002.

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ABSTRACT Escherichia coli K-12 can ferment l-ascorbate. The operon encoding catabolic enzymes in the utilization of l-ascorbate (ula) has been identified; this operon of previously unknown function had been designated the yif-sga operon. Three enzymes in the pathway that produce d-xylulose 5-phosphate have been functionally characterized: 3-keto-l-gulonate 6-phosphate decarboxylase (UlaD), l-xylulose 5-phosphate 3-epimerase (UlaE), and l-ribulose 5-phosphate 4-epimerase (UlaF). Several products of the yia-sgb operon were also functionally characterized, although the substrate and physiological
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Peleato, Maria Luisa, Teresa Muiño-Blanco, José Alvaro Cebrian Pérez, and Manuel José López-Pérez. "Significance of the Non-Oxidative Pentose Phosphate Pathway in Aspergillus oryzae Grown on Different Carbon Sources." Zeitschrift für Naturforschung C 46, no. 3-4 (1991): 223–27. http://dx.doi.org/10.1515/znc-1991-3-411.

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Specific enzyme activities of the non-oxidative pentose phosphate pathway in Aspergillus oryzae mycelia grown on different carbon sources were determined. Mycelia grown on glucose, mannitol and ribose show the highest specific activities, ribose 5-phosphate isomerase being specially very enhanced. Moreover, transketolase, transaldolase, ribose 5-phosphate isomerase and ribulose 5-phosphate 3-epimerase were determined in different developmental stages of mycelia grown on glucose, mannitol and ribose. The non-oxidative pentose phosphate pathway is more active during conidiogenesis, except for ri
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Ibañez, Ester, Rosa Gimenez, Tomas Pedraza, Laura Baldoma, Juan Aguilar, and Josefa Badia. "Role of the yiaR and yiaSGenes of Escherichia coli in Metabolism of Endogenously Formed l-Xylulose." Journal of Bacteriology 182, no. 16 (2000): 4625–27. http://dx.doi.org/10.1128/jb.182.16.4625-4627.2000.

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ABSTRACT Genes yiaP and yiaR of theyiaKLMNOPQRS cluster of Escherichia coli are required for the metabolism of the endogenously formedl-xylulose, whereas yiaS is required for this metabolism only in araD mutants. Like AraD, YiaS was shown to have l-ribulose-5-phosphate 4-epimerase activity. Similarity of YiaR to several 3-epimerases suggested that this protein could catalyze the conversion of l-xylulose-5-phosphate into l-ribulose-5-phosphate, thus completing the pathway between l-xylulose and the general metabolism.
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Wise, Eric L., Julie Akana, John A. Gerlt, and Ivan Rayment. "Structure ofD-ribulose 5-phosphate 3-epimerase fromSynechocystisto 1.6 Å resolution." Acta Crystallographica Section D Biological Crystallography 60, no. 9 (2004): 1687–90. http://dx.doi.org/10.1107/s0907444904015896.

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6

Caruthers, J., J. Bosch, F. Buckner, et al. "Structure of a ribulose 5-phosphate 3-epimerase from Plasmodium falciparum." Proteins: Structure, Function, and Bioinformatics 62, no. 2 (2005): 338–42. http://dx.doi.org/10.1002/prot.20764.

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Le, Simone Balzer, Tonje Marita Bjerkan Heggeset, Tone Haugen, Ingemar Nærdal, and Trygve Brautaset. "6-Phosphofructokinase and ribulose-5-phosphate 3-epimerase in methylotrophic Bacillus methanolicus ribulose monophosphate cycle." Applied Microbiology and Biotechnology 101, no. 10 (2017): 4185–200. http://dx.doi.org/10.1007/s00253-017-8173-0.

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8

Dallapiccola, Bruno, Giuseppe Novelli, and Aldo Giannotti. "Deletion 2q31.3?2q33.3: gene dosage effect of ribulose 5-phosphate 3-epimerase." Human Genetics 79, no. 1 (1988): 92. http://dx.doi.org/10.1007/bf00291721.

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Hennig, Guido, Carsten Haupka, Luciana F. Brito, et al. "Methanol-Essential Growth of Corynebacterium glutamicum: Adaptive Laboratory Evolution Overcomes Limitation due to Methanethiol Assimilation Pathway." International Journal of Molecular Sciences 21, no. 10 (2020): 3617. http://dx.doi.org/10.3390/ijms21103617.

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Methanol is a sustainable substrate for biotechnology. In addition to natural methylotrophs, metabolic engineering has gained attention for transfer of methylotrophy. Here, we engineered Corynebacterium glutamicum for methanol-dependent growth with a sugar co-substrate. Heterologous expression of genes for methanol dehydrogenase from Bacillus methanolicus and of ribulose monophosphate pathway genes for hexulose phosphate synthase and isomerase from Bacillus subtilis enabled methanol-dependent growth of mutants carrying one of two independent metabolic cut-offs, i.e., either lacking ribose-5-ph
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Akana, Julie, Alexander A. Fedorov, Elena Fedorov та ін. "d-Ribulose 5-Phosphate 3-Epimerase: Functional and Structural Relationships to Members of the Ribulose-Phosphate Binding (β/α)8-Barrel Superfamily†,‡". Biochemistry 45, № 8 (2006): 2493–503. http://dx.doi.org/10.1021/bi052474m.

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Book chapters on the topic "Ribulose-5-phosphate-3-epimerase"

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Kopriva, Stanislav, Anna Koprivova, and Karl-Heinz Süss. "Molecular Cloning and Characterization of Cytosolic Isoform of Ribulose-5-Phosphate 3-Epimerase from Rice." In Photosynthesis: Mechanisms and Effects. Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_820.

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"L-Ribulose-5-phosphate 3-epimerase." In Class 4–6 Lyases, Isomerases, Ligases. Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-85707-5_101.

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