Relevant bibliographies by topics / Fructose-6-phosphate phosphoketolase

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Academic literature on the topic 'Fructose-6-phosphate phosphoketolase'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Fructose-6-phosphate phosphoketolase"

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Glenn, Katie, and Kerry S. Smith. "Allosteric Regulation of Lactobacillus plantarum Xylulose 5-Phosphate/Fructose 6-Phosphate Phosphoketolase (Xfp)." Journal of Bacteriology 197, no. 7 (January 20, 2015): 1157–63. http://dx.doi.org/10.1128/jb.02380-14.

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ABSTRACTXylulose 5-phosphate/fructose 6-phosphate phosphoketolase (Xfp), which catalyzes the conversion of xylulose 5-phosphate (X5P) or fructose 6-phosphate (F6P) to acetyl phosphate, plays a key role in carbohydrate metabolism in a number of bacteria. Recently, we demonstrated that the fungalCryptococcus neoformansXfp2 exhibits both substrate cooperativity for all substrates (X5P, F6P, and Pi) and allosteric regulation in the forms of inhibition by phosphoenolpyruvate (PEP), oxaloacetic acid (OAA), and ATP and activation by AMP (K. Glenn, C. Ingram-Smith, and K. S. Smith. Eukaryot Cell13:657–663, 2014). Allosteric regulation has not been reported previously for the characterized bacterial Xfps. Here, we report the discovery of substrate cooperativity and allosteric regulation among bacterial Xfps, specifically theLactobacillus plantarumXfp.L. plantarumXfp is an allosteric enzyme inhibited by PEP, OAA, and glyoxylate but unaffected by the presence of ATP or AMP. Glyoxylate is an additional inhibitor to those previously reported forC. neoformansXfp2. As withC. neoformansXfp2, PEP and OAA share the same or possess overlapping sites onL. plantarumXfp. Glyoxylate, which had the lowest half-maximal inhibitory concentration of the three inhibitors, binds at a separate site. This study demonstrates that substrate cooperativity and allosteric regulation may be common properties among bacterial and eukaryotic Xfp enzymes, yet important differences exist between the enzymes in these two domains.IMPORTANCEXylulose 5-phosphate/fructose 6-phosphate phosphoketolase (Xfp) plays a key role in carbohydrate metabolism in a number of bacteria. Although we recently demonstrated that the fungalCryptococcusXfp is subject to substrate cooperativity and allosteric regulation, neither phenomenon has been reported for a bacterial Xfp. Here, we report that theLactobacillus plantarumXfp displays substrate cooperativity and is allosterically inhibited by phosphoenolpyruvate and oxaloacetate, as is the case forCryptococcusXfp. The bacterial enzyme is unaffected by the presence of AMP or ATP, which act as a potent activator and inhibitor of the fungal Xfp, respectively. Our results demonstrate that substrate cooperativity and allosteric regulation may be common properties among bacterial and eukaryotic Xfps, yet important differences exist between the enzymes in these two domains.
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Sánchez, Borja, Luis Noriega, Patricia Ruas-Madiedo, Clara G. Reyes-Gavilán, and Abelardo Margolles. "Acquired resistance to bile increases fructose-6-phosphate phosphoketolase activity inBifidobacterium." FEMS Microbiology Letters 235, no. 1 (June 2004): 35–41. http://dx.doi.org/10.1111/j.1574-6968.2004.tb09564.x.

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Meile, Leo, Lukas M. Rohr, Thomas A. Geissmann, Monique Herensperger, and Michael Teuber. "Characterization of the d-Xylulose 5-Phosphate/d-Fructose 6-Phosphate Phosphoketolase Gene (xfp) from Bifidobacterium lactis." Journal of Bacteriology 183, no. 9 (May 1, 2001): 2929–36. http://dx.doi.org/10.1128/jb.183.9.2929-2936.2001.

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ABSTRACT A d-xylulose 5-phosphate/d-fructose 6-phosphate phosphoketolase (Xfp) from the probioticBifidobacterium lactis was purified to homogeneity. The specific activity of the purified enzyme with d-fructose 6-phosphate as a substrate is 4.28 Units per mg of enzyme.Km values for d-xylulose 5-phosphate and d-fructose 6-phosphate are 45 and 10 mM, respectively. The native enzyme has a molecular mass of 550,000 Da. The subunit size upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis (90,000 Da) corresponds with the size (92,529 Da) calculated from the amino acid sequence of the isolated gene (namedxfp) encoding 825 amino acids. The xfp gene was identified on the chromosome of B. lactis with the help of degenerated nucleotide probes deduced from the common N-terminal amino acid sequence of both the native and denatured enzyme. Comparison of the deduced amino acid sequence of the cloned gene with sequences in public databases revealed high homologies with hypothetical proteins (26 to 55% identity) in 20 microbial genomes. The amino acid sequence derived from the xfp gene contains typical thiamine diphosphate (ThDP) binding sites reported for other ThDP-dependent enzymes. Two truncated putative genes, pta andguaA, were localized adjacent to xfp on theB. lactis chromosome coding for a phosphotransacetylase and a guanosine monophosphate synthetase homologous to products of genes inMycobacterium tuberculosis. However, xfp is transcribed in B. lactis as a monocistronic operon. It is the first reported and sequenced gene of a phosphoketolase.
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BIBILONI, RODRIGO, PABLO F. PÉREZ, and GRACIELA L. DE ANTONI. "An Enzymatic–Colorimetric Assay for the Quantification of Bifidobacterium." Journal of Food Protection 63, no. 3 (March 1, 2000): 322–26. http://dx.doi.org/10.4315/0362-028x-63.3.322.

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An enzymatic–colorimetric assay for the quantification of Bifidobacterium was developed. The method, based upon the standard detection of fructose-6-phosphate phosphoketolase activity, was optimized with respect to bacterial cell pretreatment, time of incubation, and substrate concentration. The relationship between bacterial biomass and phosphoketolase activity was linear in a wide spectrum of bacterial densities. Higher sensitivity over the standard method was achieved by using 0.25% Triton X-100 in the reaction mixture to pretreat the bacterial cells. Because autoaggregation is a frequent feature among Bifidobacterium strains, this simple and reproducible method offers good advantage over viable plate count and turbidimetric techniques. The methodology can also be applied to the assessment of adherent Bifidobacterium strains to human epithelial cells.
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Kang, Tae Sun, Darren R. Korber, and Takuji Tanaka. "Regulation of Dual Glycolytic Pathways for Fructose Metabolism in Heterofermentative Lactobacillus panis PM1." Applied and Environmental Microbiology 79, no. 24 (October 4, 2013): 7818–26. http://dx.doi.org/10.1128/aem.02377-13.

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ABSTRACTLactobacillus panisPM1 belongs to the group III heterofermentative lactobacilli that use the 6-phosphogluconate/phosphoketolase (6-PG/PK) pathway as their central metabolic pathway and are reportedly unable to grow on fructose as a sole carbon source. We isolated a variant PM1 strain capable of sporadic growth on fructose medium and observed its distinctive characteristics of fructose metabolism. The end product pattern was different from what is expected in typical group III lactobacilli using the 6-PG/PK pathway (i.e., more lactate, less acetate, and no mannitol). In addition,in silicoanalysis revealed the presence of genes encoding most of critical enzymes in the Embden-Meyerhof (EM) pathway. These observations indicated that fructose was metabolized via two pathways. Fructose metabolism in the PM1 strain was influenced by the activities of two enzymes, triosephosphate isomerase (TPI) and glucose 6-phosphate isomerase (PGI). A lack of TPI resulted in the intracellular accumulation of dihydroxyacetone phosphate (DHAP) in PM1, the toxicity of which caused early growth cessation during fructose fermentation. The activity of PGI was enhanced by the presence of glyceraldehyde 3-phosphate (GAP), which allowed additional fructose to enter into the 6-PG/PK pathway to avoid toxicity by DHAP. Exogenous TPI gene expression shifted fructose metabolism from heterolactic to homolactic fermentation, indicating that TPI enabled the PM1 strain to mainly use the EM pathway for fructose fermentation. These findings clearly demonstrate that the balance in the accumulation of GAP and DHAP determines the fate of fructose metabolism and the activity of TPI plays a critical role during fructose fermentation via the EM pathway inL. panisPM1.
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Glenn, Katie, Cheryl Ingram-Smith, and Kerry S. Smith. "Biochemical and Kinetic Characterization of Xylulose 5-Phosphate/Fructose 6-Phosphate Phosphoketolase 2 (Xfp2) from Cryptococcus neoformans." Eukaryotic Cell 13, no. 5 (March 21, 2014): 657–63. http://dx.doi.org/10.1128/ec.00055-14.

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ABSTRACTXylulose 5-phosphate/fructose 6-phosphate phosphoketolase (Xfp), previously thought to be present only in bacteria but recently found in fungi, catalyzes the formation of acetyl phosphate from xylulose 5-phosphate or fructose 6-phosphate. Here, we describe the first biochemical and kinetic characterization of a eukaryotic Xfp, from the opportunistic fungal pathogenCryptococcus neoformans, which has twoXFPgenes (designatedXFP1andXFP2). Our kinetic characterization ofC. neoformansXfp2 indicated the existence of both substrate cooperativity for all three substrates and allosteric regulation through the binding of effector molecules at sites separate from the active site. Prior to this study, Xfp enzymes from two bacterial genera had been characterized and were determined to follow Michaelis-Menten kinetics.C. neoformansXfp2 is inhibited by ATP, phosphoenolpyruvate (PEP), and oxaloacetic acid (OAA) and activated by AMP. ATP is the strongest inhibitor, with a half-maximal inhibitory concentration (IC50) of 0.6 mM. PEP and OAA were found to share the same or have overlapping allosteric binding sites, while ATP binds at a separate site. AMP acts as a very potent activator; as little as 20 μM AMP is capable of increasing Xfp2 activity by 24.8% ± 1.0% (mean ± standard error of the mean), while 50 μM prevented inhibition caused by 0.6 mM ATP. AMP and PEP/OAA operated independently, with AMP activating Xfp2 and PEP/OAA inhibiting the activated enzyme. This study provides valuable insight into the metabolic role of Xfp within fungi, specifically the fungal pathogenCryptococcus neoformans, and suggests that at least some Xfps display substrate cooperative binding and allosteric regulation.
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Suzuki, Ryuichiro, Byung-Jun Kim, Tsuyoshi Shibata, Yuki Iwamoto, Takane Katayama, Hisashi Ashida, Takayoshi Wakagi, Hirofumi Shoun, Shinya Fushinobu, and Kenji Yamamoto. "Overexpression, crystallization and preliminary X-ray analysis of xylulose-5-phosphate/fructose-6-phosphate phosphoketolase fromBifidobacterium breve." Acta Crystallographica Section F Structural Biology and Crystallization Communications 66, no. 8 (July 29, 2010): 941–43. http://dx.doi.org/10.1107/s1744309110023845.

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8

Fandi, K. G., H. M. Ghazali, A. M. Yazid, and A. R. Raha. "Purification and N-terminal amino acid sequence of fructose-6-phosphate phosphoketolase from Bifidobacterium longum BB536." Letters in Applied Microbiology 32, no. 4 (April 11, 2001): 235–39. http://dx.doi.org/10.1046/j.1472-765x.2001.00895.x.

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9

Gavini, F., M. Van Esbroeck, J. P. Touzel, A. Fourment, and H. Goossens. "Detection of Fructose-6-phosphate Phosphoketolase (F6PPK), a Key Enzyme of the Bifid-Shunt, inGardnerella vaginalis." Anaerobe 2, no. 3 (June 1996): 191–93. http://dx.doi.org/10.1006/anae.1996.0025.

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10

Bolado-Martínez, E., E. Acedo-Félix, A. B. Peregrino-Uriarte, and G. Yepiz-Plascencia. "Fructose 6-phosphate phosphoketolase activity in wild-type strains of Lactobacillus, isolated from the intestinal tract of pigs." Applied Biochemistry and Microbiology 48, no. 5 (September 2012): 444–51. http://dx.doi.org/10.1134/s000368381205002x.

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Dissertations / Theses on the topic "Fructose-6-phosphate phosphoketolase"

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Grill, Jean-Pierre. "Étude du potentiel probiotique de bactéries du genre Bifidobacterium : purification et caractérisation de la fructose 6 phosphate phosphocetolase de Bifidobacterium longum et Bifidobacterium animalis." Nancy 1, 1995. http://www.theses.fr/1995NAN10050.

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Cette étude a permis de montrer les effets de certaines souches de bactéries appartenant au genre Bifidobacterium sur la flore intestinale, les nitrites, les nitrosamines et les sels biliaires. L’enzyme impliquée dans la déconjugaison des sels biliaires a été purifiée et caractérisée pour la souche de Bifidobacterium longum BB536. La fructose 6 phosphate phosphocétolase a été purifiée et caractérisée chez différentes souches de bifidobactéries. Des séquences en acides aminés de cette protéine ont ainsi été obtenues pour Bifidobacterium longum et Bifidobacterium animalis
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Book chapters on the topic "Fructose-6-phosphate phosphoketolase"

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Schomburg, Dietmar, and Margit Salzmann. "Fructose-6-phosphate phosphoketolase." In Enzyme Handbook 1, 357–60. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_81.

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