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Journal articles on the topic 'Glucose phosphate isomerase'

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Published: 4 June 2021

Last updated: 4 February 2022

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1

Yeom, Soo-Jin, Yeong-Su Kim, and Deok-Kun Oh. "Development of Novel Sugar Isomerases by Optimization of Active Sites in Phosphosugar Isomerases for Monosaccharides." Applied and Environmental Microbiology 79, no. 3 (November 30, 2012): 982–88. http://dx.doi.org/10.1128/aem.02539-12.

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ABSTRACTPhosphosugar isomerases can catalyze the isomerization of not only phosphosugar but also of monosaccharides, suggesting that the phosphosugar isomerases can be used as sugar isomerases that do not exist in nature. Determination of active-site residues of phosphosugar isomerases, including ribose-5-phosphate isomerase fromClostridium difficile(CDRPI), mannose-6-phosphate isomerase fromBacillus subtilis(BSMPI), and glucose-6-phosphate isomerase fromPyrococcus furiosus(PFGPI), was accomplished by docking of monosaccharides onto the structure models of the isomerases. The determinant residues, including Arg133 of CDRPI, Arg192 of BSMPI, and Thr85 of PFGPI, were subjected to alanine substitutions and found to act as phosphate-binding sites. R133D of CDRPI, R192 of BSMPI, and T85Q of PFGPI displayed the highest catalytic efficiencies for monosaccharides at each position. These residues exhibited 1.8-, 3.5-, and 4.9-fold higher catalytic efficiencies, respectively, for the monosaccharides than the wild-type enzyme. However, the activities of these 3 variant enzymes for phosphosugars as the original substrates disappeared. Thus, R133D of CDRPI, R192 of BSMPI, and T85Q of PFGPI are no longer phosphosugar isomerases; instead, they are changed to ad-ribose isomerase, anl-ribose isomerase, and anl-talose isomerase, respectively. In this study, we used substrate-tailored optimization to develop novel sugar isomerases which are not found in nature based on phosphosugar isomerases.

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2

Kugler, Wilfried, and Max Lakomek. "Glucose-6-phosphate isomerase deficiency." Best Practice & Research Clinical Haematology 13, no. 1 (March 2000): 89–101. http://dx.doi.org/10.1053/beha.1999.0059.

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3

MORGAN, MICHAEL J., JAMES I. H. WALKER, ALISON A. M. REDMILL, and PELIN FAIK. "Molecular genetics of glucose phosphate isomerase." Biochemical Society Transactions 18, no. 2 (April 1, 1990): 183–84. http://dx.doi.org/10.1042/bst0180183.

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4

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 (April 1, 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 ribulose 5-phosphate 3-epimerase, suggesting a fundamental role of this pathway during that stage to supply pentoses for nucleic acids biosynthesis. A general decrease of the enzyme activities was found in sporulated mycelia. Arabinose 5-phosphate was tested as metabolite of the pentose pathway. This pentose phosphate was not converted into hexose phosphates or triose phosphates and inhibits significantly the ribose 5-phosphate utilization, being therefore unappropriate to support the Aspergillus oryzae growth.

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5

Hassett, Sylvia W., David E. McMillin, and Jerry W. Johnson. "Aconitase and glucose phosphate isomerase variation in hexaploid wheat." Canadian Journal of Plant Science 73, no. 3 (July 1, 1993): 743–48. http://dx.doi.org/10.4141/cjps93-097.

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The purpose of this study was to determine if isozyme variation could be found in wheat (Triticum aestivum L. em. Thell) for the isozymes aconitase, alcohol dehydrogenase and glucose phosphate isomerase; these isozymes are encoded by genes on wheat chromosomes with loci conferring pest resistance. Two hundred and fifty wheat accessions were examined for variation in the isozymes aconitase and alcohol dehydrogenase using starch gel electrophoresis. Accessions were chosen at random from a collection of hexaploid wheat lines from all over the world. In addition, twenty-one accessions which exhibited unusual variation for either endopeptidase or aconitase were examined for glucose phosphate isomerase variation using isoelectric focusing. While no isozyme variation was seen for alcohol dehydrogenase, variation was detected for aconitase and glucose phosphate isomerase. In addition, the glucose phosphate isomerase phenotypes of wheat lines with the 1B-1Rs and 1A-1Rs wheat-rye translocations were distinguished. Therefore, evaluation of glucose phosphate phenotypes could potentially be used in wheat improvement programs to identify plants which are homozygous for wheat-rye translocations involving chromosome 1. Key words: Triticum aestivum, isozyme variation, wheat improvement

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6

Forsyth, R. J., K. Bartlett, A. Burchell, H. M. Scott, and J. A. Eyre. "Astrocytic glucose-6-phosphatase and the permeability of brain microsomes to glucose 6-phosphate." Biochemical Journal 294, no. 1 (August 15, 1993): 145–51. http://dx.doi.org/10.1042/bj2940145.

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Cells from primary rat astrocyte cultures express a 36.5 kDa protein that cross-reacts with polyclonal antibodies to the catalytic subunit of rat hepatic glucose-6-phosphatase on Western blotting. Glucose-6-phosphate-hydrolysing activity of the order of 10 nmol/min per mg of total cellular protein can be demonstrated in cell homogenates. This activity shows latency, and is localized to the microsomal fraction. Kinetic analysis shows a Km of 15 mM and a Vmax. of 30 nmol/min per mg of microsomal protein in disrupted microsomes. Approx. 40% of the total phosphohydrolase activity is specific glucose-6-phosphatase, as judged by sensitivity to exposure to pH 5 at 37 degrees C. Previous reports that the brain microsomal glucose-6-phosphatase system does not distinguish glucose 6-phosphate and mannose 6-phosphate are confirmed in astrocyte microsomes. However, we demonstrate significant phosphomannose isomerase activity in brain microsomes, allowing for ready interconversion between mannose 6-phosphate and glucose 6-phosphate (Vmax. 15 nmol/min per mg of microsomal protein; apparent Km < 1 mM; pH optimum 5-6 for the two-step conversion). This finding invalidates the past inference from the failure of brain microsomes to distinguish mannose 6-phosphate and glucose 6-phosphate that the cerebral glucose-6-phosphatase system lacks a ‘glucose 6-phosphate translocase’ [Fishman and Karnovsky (1986) J. Neurochem. 46, 371-378]. Furthermore, light-scattering experiments confirm that a proportion of whole brain microsomes is readily permeable to glucose 6-phosphate.

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7

Munikoty, Vinay, D. Tarangini, Vandana Bharadwaj, and Anand Prakash. "The ‘After Thought’ Enzyme: Glucose Phosphate Isomerase (GPI)." Pediatric Hematology Oncology Journal 3, no. 3 (2018): S40. http://dx.doi.org/10.1016/j.phoj.2018.11.115.

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8

Simon, L. M., M. Kotormán, B. Szajáni, and L. Boross. "Preparation and characterization of immobilized glucose-phosphate isomerase." Enzyme and Microbial Technology 8, no. 4 (April 1986): 222–26. http://dx.doi.org/10.1016/0141-0229(86)90092-x.

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9

Rajendram, G. F. "ELECTROPHORETIC STUDY OF ENZYMES FROM A GLOSSINA FUSCIPES FUSCIPES NEWSTEAD POPULATION FROM WESTERN KENYA." Canadian Entomologist 123, no. 2 (April 1991): 295–98. http://dx.doi.org/10.4039/ent123295-2.

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AbstractEnzymes were investigated, by electrophoresis, in a population of Glossina fuscipes fuscipes Newstead collected from Rusinga Island in Lake Victoria, Western Kenya.The following enzymes were tested: glucose phosphate isomerase, glucose-6-phosphate dehydrogenase (G6PDH), hexokinase. isocitrate dehydrogenase (IDH), malate-dehydrogenase (MDH), phosphoglucomutase, and xanthine dehydrogenase (XDH).Single monomorphic bands were stained by the following enzymes apparently under the control of single loci: G6PDH, MDH, and XDH. The enzyme IDH showed two bands with very close mobilities and no variation among individuals in the population. Hence IDH was considered as representing a single locus. Glucose phosphate isomerase manifested three alleles and apparently six genotypes. Phosphoglucomutase manifested a double-banded pattern representing an autosomal locus.

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10

Hua, Qiang, Chen Yang, Tomoya Baba, Hirotada Mori, and Kazuyuki Shimizu. "Responses of theCentral Metabolism in Escherichia coli to PhosphoglucoseIsomerase and Glucose-6-Phosphate DehydrogenaseKnockouts." Journal of Bacteriology 185, no. 24 (December 15, 2003): 7053–67. http://dx.doi.org/10.1128/jb.185.24.7053-7067.2003.

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ABSTRACT The responses of Escherichia coli central carbon metabolism to knockout mutations in phosphoglucose isomerase and glucose-6-phosphate (G6P) dehydrogenase genes were investigated by using glucose- and ammonia-limited chemostats. The metabolic network structures and intracellular carbon fluxes in the wild type and in the knockout mutants were characterized by using the complementary methods of flux ratio analysis and metabolic flux analysis based on [U-13C]glucose labeling and two-dimensional nuclear magnetic resonance (NMR) spectroscopy of cellular amino acids, glycerol, and glucose. Disruption of phosphoglucose isomerase resulted in use of the pentose phosphate pathway as the primary route of glucose catabolism, while flux rerouting via the Embden-Meyerhof-Parnas pathway and the nonoxidative branch of the pentose phosphate pathway compensated for the G6P dehydrogenase deficiency. Furthermore, additional, unexpected flux responses to the knockout mutations were observed. Most prominently, the glyoxylate shunt was found to be active in phosphoglucose isomerase-deficient E. coli. The Entner-Doudoroff pathway also contributed to a minor fraction of the glucose catabolism in this mutant strain. Moreover, although knockout of G6P dehydrogenase had no significant influence on the central metabolism under glucose-limited conditions, this mutation resulted in extensive overflow metabolism and extremely low tricarboxylic acid cycle fluxes under ammonia limitation conditions.

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11

Horáček, J., and M. Ačanová. "Glucose-6-phosphate Isomerase as a Marker of a Fertility Restorer Gene in Rape – Short Communication." Czech Journal of Genetics and Plant Breeding 39, No. 4 (November 23, 2011): 130–33. http://dx.doi.org/10.17221/3731-cjgpb.

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 In breeding of winter rape (Brassica napus L. var. napus) using the OGU-INRA system, based on cytoplasmic male sterility (CMS), it is necessary to distinguish pollen-sterile lines, carrying CMS factors and the recessive fertility restorer alleles rfrf, from fertile lines, carrying at least one dominant restorer gene allele (Rfrf or RfRf). To grow plants till the flowering stage takes much time. The method was therefore modified using isozyme markers of glucose-6-phosphate isomerase (PGI) to distinguish male sterile (MS) from male-fertile lines in early stages. Since the restorer gene is tightly linked to the markers and the PGI isozymes can be distinguished by electrophoresis, the markers can be used to identify MS rape plants in early stages. Also, homozygous and heterozygous fertility-restored plants can be separated this way. In our work we tried to optimise the distinction of pollen-fertile and pollen-sterile rape plants with PGI isozyme markers, using vertical polyacrylamide gel electrophoresis (native-PAGE). The method will be used for the breeding of rapeseed with the OGU-INRA system.  

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12

Hirano, Hisashi, Ritsuko Murakami, Hiroaki Yamanouchi, and Taiji Emoto. "Polymorphism of glucose phosphate isomerase from mulberry (Morus spp.)." SEIBUTSU BUTSURI KAGAKU 46, no. 1 (2002): 15–18. http://dx.doi.org/10.2198/sbk.46.15.

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13

Mahalingam, Soundarya, and L. Harshaprasada. "Nonspherocytic Hemolytic Anemia Due To Glucose Phosphate Isomerase Deficiency." Pediatric Hematology Oncology Journal 3, no. 3 (2018): S34. http://dx.doi.org/10.1016/j.phoj.2018.11.097.

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14

WEGHE, A., TS YABLANSKI, A. ZEVEREN, and Y. BOUQUET. "A third variant of glucose phosphate isomerase in pigs." Animal Genetics 19, no. 1 (April 24, 2009): 55–58. http://dx.doi.org/10.1111/j.1365-2052.1988.tb00790.x.

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15

ARNOLD, I. C. J., and J. BOUW. "A new allele of glucose phosphate isomerase in dogs." Animal Genetics 20, no. 3 (April 24, 2009): 217–20. http://dx.doi.org/10.1111/j.1365-2052.1989.tb00860.x.

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16

Razmjou, Elham, Ali Haghighi, Mostafa Rezaian, Seiki Kobayashi, and Tomoyoshi Nozaki. "Genetic diversity of glucose phosphate isomerase from Entamoeba histolytica." Parasitology International 55, no. 4 (December 2006): 307–11. http://dx.doi.org/10.1016/j.parint.2006.08.001.

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17

XU, WEIMING, PAULINE LEE, and ERNEST BEUTLER. "Human Glucose Phosphate Isomerase: Exon Mapping and Gene Structure." Genomics 29, no. 3 (October 1995): 732–39. http://dx.doi.org/10.1006/geno.1995.9944.

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18

Cech, David L., Pan-Fen Wang, Melissa C. Holt, Victoria A. Assimon, Jeffrey M. Schaub, Tod P. Holler, and Ronald W. Woodard. "A Novel Glucose 6-Phosphate Isomerase from Listeria monocytogenes." Protein Journal 33, no. 5 (September 7, 2014): 447–56. http://dx.doi.org/10.1007/s10930-014-9577-7.

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19

Smith, Michael W., and Russell F. Doolittle. "Anomalous phylogeny involving the enzyme glucose-6-phosphate isomerase." Journal of Molecular Evolution 34, no. 6 (June 1992): 544–45. http://dx.doi.org/10.1007/bf00160467.

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20

Hattori, Jiro, Bernard R. Baum, and Brian L. Miki. "Ancient diversity of the glucose-6-phosphate isomerase genes." Biochemical Systematics and Ecology 23, no. 1 (January 1995): 33–38. http://dx.doi.org/10.1016/0305-1978(95)93658-p.

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21

Sène, M., P. Brémond, J. P. Hervé, V. R. Southgate, B. Sellin, B. Marchand, and J. M. Duplantier. "Comparison of human and murine isolates of Schistosoma mansoni from Richard-Toll, Senegal, by isoelectric focusing." Journal of Helminthology 71, no. 2 (June 1997): 175–81. http://dx.doi.org/10.1017/s0022149x00015868.

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AbstractStudies on human and murine isolates of Schistosoma mansoni, from Richard-Toll, Senegal, were carried out by isoelectric focusing in polyacrylamide gels. Seven enzyme systems; lactate dehydrogenase (LDH), malate dehydrogenase (MDH), glucose-6-phosphate dehydrogenase (G6PD), acid phosphatase (AcP), hexokinase (HK), glucose phosphate isomerase (GPI), and phosphoglucomutase (PGM), were used to compare the two isolates. All systems tested, apart from LDH, were found to be polymorphic for both isolates. Interestingly, one phenotype is more frequent than the remainder. The results show that there is no significant genetic variation between the S. mansoni isolates from man and the rodents, Arvicanthis niloticus and Mastomys huberti.

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22

Willem, R., F. Malaisse-Lagae, R. Ottinger, and W. J. Malaisse. "Phosphoglucoisomerase-catalysed interconversion of hexose phosphates. Kinetic study by 13C n.m.r. of the phosphoglucoisomerase reaction in 2H2O." Biochemical Journal 265, no. 2 (January 15, 1990): 519–24. http://dx.doi.org/10.1042/bj2650519.

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The fate of D-[2-13C]glucose 6-phosphate exposed to phosphoglucoisomerase (glucose-6-phosphate isomerase, EC 5.3.1.9) in 2H2O was monitored by 13C-n.m.r. spectroscopy. The generation of the anomers of both D-[2-13C]fructose 6-phosphate and D-[2-13C,2-2H]glucose 6-phosphate followed a single-exponential pattern. The rate constant, which was proportional to the enzyme concentration, was about 14 times higher, however, in the former than in the latter case. The disappearance of D-[2-13C,2-1H]glucose 6-phosphate occurred in a bi-exponential manner, the rate constants for the fast and the slow processes being in fair agreement with those obtained for the generation of D-[2-13C]fructose 6-phosphate and D-[2-13C,2-2H]glucose 6-phosphate respectively. These findings indicate that the process of equilibration of D-[2-13C]glucose 6-phosphate and D-[2-13C]fructose 6-phosphate is at least one order of magnitude faster than the intermolecular proton transfer involving the deuterons from the solvent. Such a difference provides strong support to the view that the inverconversion of hexose phosphates in the reaction catalysed by phosphoglucoisomerase proceeds in two distinct steps, the second of which occurs according to two competing modalities with either an intramolecular or an intermolecular proton transfer.

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23

Kowallik, Wolfgang, Meinolf Thiemann, Yi Huang, Gerard Mutumba, Lisa Beermann, Dagmar Broer, and Norbert Grotjohann. "Complete Sequence of Glycolytic Enzymes in the Mycorrhizal Basidiomycete, Suillus bovinus." Zeitschrift für Naturforschung C 53, no. 9-10 (October 1, 1998): 818–27. http://dx.doi.org/10.1515/znc-1998-9-1007.

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Axenic cultures of Suillus bovinus were cultivated in inorganic liquid medium with glucose as a carbon source at 25 °C and continuous supply of oxygen by aeration with compressed air in the dark. Exogenous fructose as sole carbon source yielded about 50% less increase in dry weight than glucose. This resulted from different uptake velocities. Sucrose as sole exogenous carbon source yielded no measurable increase in dry weight. In glucose cultures, activities of all glycolytic enzymes were found. Maximum specific activities varied largely (from about 60 [fructose 6-phosphate kinase] to about 20 000 [triosephosphate isomerase] nmoles · mg protein-1 · min-1). Apparent Km-values also varied over more than two orders of magnitude (0.035 mᴍ [pyruvate kinase] to 6.16 mᴍ [triosephosphate isomerase]). Fructose 6-phosphate kinase proved to be the fructose 2,6-bisphosphate-regulated type, aldolase the divalent cation-dependent (class II) type and glyceratephosphate mutase the glycerate 2,3-phosphate-independent type of the respective enzymes. Eight of the 10 enzymes exhibited pʜ-optima′ between 7.5-8.0. Triosephosphate isomerase and pyruvate kinase showed highest activities at pʜ 6.5. Regulatory sites within the glycolytic pathway of Suillus bovinus are discussed; fructose 6-phosphate kinase appears to be its main bottle neck.

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24

Lunn, J. E., and T. ap Rees. "Apparent equilibrium constant and mass-action ratio for sucrose-phosphate synthase in seeds of Pisum sativum." Biochemical Journal 267, no. 3 (May 1, 1990): 739–43. http://dx.doi.org/10.1042/bj2670739.

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The aim of this work was to use preparations from germinating seeds of Pisum sativum to determine the apparent equilibrium constant of the reaction catalysed by sucrose-phosphate synthase (EC 2.4.1.14) and to compare this with the mass-action ratio of the reaction in the seeds. The apparent equilibrium constant ranged from 5.3 at 0.25 mM-MgCl2, pH 7.0, to 62 at 10 mM-MgCl2, pH 7.5. The sucrose phosphate content of the seeds, 23 nmol/g fresh wt., was determined by separating sucrose phosphate from sucrose by ion-exchange chromatography and then measuring the sucrose released by alkaline phosphatase. Comparison of equilibrium constants and mass-action ratios in the cotyledons of 38 h-germinated seeds showed that the reactions catalysed by glucose-6-phosphate isomerase, phosphoglucomutase and UDP-glucose pyrophosphorylase are close to equilibrium, and those catalysed by sucrose-phosphate synthase and sucrose phosphatase are considerably displaced from equilibrium in vivo.

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25

COX, T. S., J. P. MURPHY, and L. G. HARRELL. "ISOELECTRIC FOCUSING PATTERNS OF KERNEL ISOZYMES FROM 80 NORTH AMERICAN WINTER WHEAT CULTIVARS." Canadian Journal of Plant Science 68, no. 1 (January 1, 1988): 65–72. http://dx.doi.org/10.4141/cjps88-007.

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The cataloguing of wheat (Triticum aestivum L.) cultivar isozyme patterns, though a routine exercise, provides useful data for genetic and breeding studies. Isozymes of five kernel enzyme systems (β-amylase, esterases, malate dehydrogenase, superoxide dismutase, and glucose phosphate isomerase) were separated by isoelectric fosusing (IEF) for 80 North American winter wheat cultivars. No variation in malate dehydrogenase, superoxide dismutase, or glucose phosphate isomerase IEF patterns was detected. There were three groups of hard red winter wheat cultivars with esterase patterns that differed from the pattern common to all others: Arkan and Sage; Siouxland, Colt, and Pioneer 2157; and Sandy. Esterase IEF, in contrast to gliadin electrophoresis in other studies, distinguished Sage from Eagle and Larned. Four soft red winter cultivars (Compton and Adena; Florida 302; Roland) and six groups containing a total of eight hard red winter cultivars (RHS812; RHS830; Norstar; Plainsman V; TAM 105, TAM 107, and Rose; and TAM 101) had variant β-amylase patterns. Some of the esterase and β-amylase varients, produced by genes on chromosomes 3A, 3D, 4D, 5A, and possibly others, may be useful in linkage studies.Key words: Cultivar identification, electrophoresis, β-amylase, esterase, superoxide dismutase, glucose phosphate isomerase

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26

Varga, Viola, Zsófia Murányi, Anita Kurucz, Paola Marcolongo, Angelo Benedetti, Gábor Bánhegyi, and Éva Margittai. "Species-Specific Glucose-6-Phosphatase Activity in the Small Intestine—Studies in Three Different Mammalian Models." International Journal of Molecular Sciences 20, no. 20 (October 11, 2019): 5039. http://dx.doi.org/10.3390/ijms20205039.

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Besides the liver, which has always been considered the major source of endogenous glucose production in all post-absorptive situations, kidneys and intestines can also produce glucose in blood, particularly during fasting and under protein feeding. However, observations gained in different experimental animals have given ambiguous results concerning the presence of the glucose-6-phosphatase system in the small intestine. The aim of this study was to better define the species-related differences of this putative gluconeogenic organ in glucose homeostasis. The components of the glucose-6-phosphatase system (i.e., glucose-6-phosphate transporter and glucose-6-phosphatase itself) were analyzed in homogenates or microsomal fractions prepared from the small intestine mucosae and liver of rats, guinea pigs, and humans. Protein and mRNA levels, as well as glucose-6-phosphatase activities, were detected. The results showed that the glucose-6-phosphatase system is poorly represented in the small intestine of rats; on the other hand, significant expressions of glucose-6-phosphate transporter and of the glucose-6-phosphatase were found in the small intestine of guinea pigs and homo sapiens. The activity of the recently described fructose-6-phosphate transporter–intraluminal hexose isomerase pathway was also present in intestinal microsomes from these two species. The results demonstrate that the gluconeogenic role of the small intestine is highly species-specific and presumably dependent on feeding behavior (e.g., fructose consumption) and the actual state of metabolism.

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27

Torres, N. V., F. Mateo, E. Meléndez-Hevia, and H. Kacser. "Kinetics of metabolic pathways. A system in vitro to study the control of flux." Biochemical Journal 234, no. 1 (February 15, 1986): 169–74. http://dx.doi.org/10.1042/bj2340169.

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A method for determining Control Coefficients is proposed for systems studied in vitro and applied to a model pathway. Rat liver extract, which converts glucose into glycerol 3-phosphate, was used with the addition to the incubation mixture of fructose-bisphosphate aldolase, triose-phosphate isomerase and glycerol-3-phosphate dehydrogenase as ‘auxiliary’ enzymes, which leaves all the control on the first three enzymes. The flux of the metabolic pathway was recorded by assaying NADH decay. Flux Control Coefficients (CJE) of hexokinase, glucose-6-phosphate isomerase and phosphofructokinase were calculated by titration of the system with increasing quantities of extraneous enzymes. It is shown that the summation property is fulfilled. The applicability of this procedure to study the control in any metabolic pathway is discussed. Possible relevance of the method to conditions in vivo and its limitations are considered.

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28

Penteado, Maria Isabel de O., Pedro García, and Marcelino Pérez de la Vega. "Isozyme markers and genetic variability in three species of Centrosema (Leguminosae)." Brazilian Journal of Genetics 20, no. 3 (September 1997): 443–52. http://dx.doi.org/10.1590/s0100-84551997000300015.

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Isozyme patterns and their genetic control in three Centrosema species are described. Seven isozymatic systems (aspartate aminotransferase, glucose-6-phosphate isomerase, phosphoglucomutase, anodal peroxidase, malate dehydrogenase, 6-phosphogluconate dehydrogenase, and isocitrate dehydrogenase) were studied in 18 populations and several breeding lines of C. acutifolium, C. brasilianum and C. pubescens, using starch gel electrophoresis techniques. All systems, except glucose-6-phosphate isomerase, are described for the first time in these species. A total of 17 isozyme loci were scored; this represents the largest set of Mendelian loci known up to now in Centrosema species. Isozyme polymorphism and variability within and between populations and species were relatively high and allowed discrimination among species

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29

Bera, Debabrata. "KINETIC STUDY COMPARISON OF IMMOBILIZED GLUCOSE ISOMERASE (GENSWEET AND SWEETZYME IT) IN STIRRED TANK REACTOR AND PACKED BED REACTOR." Journal of Medical pharmaceutical and allied sciences 10, no. 4 (August 15, 2021): 3115–19. http://dx.doi.org/10.22270/jmpas.v10i4.1387.

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D- Glucose/xylose isomerase catalysis the reversible isomerization of aldoses to ketoses such as D-glucose and D-xylose to D-fructose and D-xylose respectively. High fructose corn syrup (HFCS), a low calorie sugar substitute for cane sugar, utilizes Glucose isomerase enzyme for conversion of glucose to fructose. The conversion of glucose to fructose favours more at high temperature, providing an incentive to utilize thermostable and thermoactive glucose isomerase in High fructose corn syrup (HFCS) production. Present studies emphasize on enzymatic conversion and optimization using Sweetzyme IT extra & Gensweet, commercially available glucose isomerases. The experiments were carried out for enzymatic conversion of glucose to fructose using Gensweet and Sweetzyme in Packed bed reactor (PBR) and Stirred tank reactor (STR). Maximum conversion was seen in Stirred tank reactor (STR) using both of these enzymes, approx 10 % more Fructose conversion comparing it to packed bed reactor (PBR). Also, Stirred tank reactor (STR) reaction conditions such as pH, buffers, cofactor (MgSO4) requirement were optimized to achieve optimum enzyme activity. Analysis of enzymatic conversion samples was done using HPLC-RID (using Zorbax Column). The importance of the divalent cation MgCl2 for optimal enzyme activity was investigated. The enzyme performed best at pH 7.5 and 60°C, using 10mM MgSO4 as a cofactor. Utilizing Gensweet in Stirred tank reactor (STR), the maximum fructose transformation was 44 %. The most activity was detected with Sodium phosphate buffers, and EPPS buffers at pH 7 and 8, accordingly, whereas the least activity was reported with TRIS HCl buffer.

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30

Walker, J. I. H., D. M. Layton, A. J. Bellingham, M. J. Morgan, and P. Faik. "DNA sequence abnormalities in human glucose 6-phosphate isomerase deficiency." Human Molecular Genetics 2, no. 3 (1993): 327–29. http://dx.doi.org/10.1093/hmg/2.3.327.

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31

Fujii, Hisaichi, Hitoshi Kanno, Akira Hirono, and Shiro Miwa. "Hematologically Important Mutations: Molecular Abnormalities of Glucose Phosphate Isomerase Deficiency." Blood Cells, Molecules, and Diseases 22, no. 2 (August 1996): 96–97. http://dx.doi.org/10.1006/bcmd.1996.0014.

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32

Oya, M., N. Komatsu, Y. Kimura, and A. Kido. "Glucose phosphate isomerase variants in human bloodstains and seminal stains." Forensic Science International 39, no. 1 (October 1988): 55–58. http://dx.doi.org/10.1016/0379-0738(88)90117-x.

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33

Ravindranath, Yaddanapudi, Donald E. Paglia, Indira Warrier, William Valentine, Misae Nakatani, and Richard A. Brockway. "Glucose Phosphate Isomerase Deficiency as a Cause of Hydrops Fetalis." New England Journal of Medicine 316, no. 5 (January 29, 1987): 258–61. http://dx.doi.org/10.1056/nejm198701293160506.

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34

Alfinito, F., F. Ferraro, S. Rocco, E. Vendittis, G. Piccirillo, A. Sementa, M. B. Colombo, A. Zanella, and B. Rotoli. "Glucose phosphate isomerase (GPI) “Morcone”: A new variant from Italy." European Journal of Haematology 52, no. 5 (April 24, 2009): 263–66. http://dx.doi.org/10.1111/j.1600-0609.1994.tb00094.x.

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35

SRIVASTAVA, I., M. SCHMIDT, M. GRALL, U. CERTA, A. GARCIA, and L. PERRIN. "Identification and purification of glucose phosphate isomerase of Plasmodium falciparum." Molecular and Biochemical Parasitology 54, no. 2 (September 1992): 153–64. http://dx.doi.org/10.1016/0166-6851(92)90108-v.

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36

Fan, Lie Ying, Ming Zong, Qiang Wang, Lin Yang, Li Shan Sun, Qin Ye, Yuan Yuan Ding, and Jian Wei Ma. "Diagnostic value of glucose-6-phosphate isomerase in rheumatoid arthritis." Clinica Chimica Acta 411, no. 23-24 (December 2010): 2049–53. http://dx.doi.org/10.1016/j.cca.2010.08.043.

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37

West, J. D., and J. H. Flockhart. "Genetic differences in glucose phosphate isomerase activity among mouse embryos." Development 107, no. 3 (November 1, 1989): 465–72. http://dx.doi.org/10.1242/dev.107.3.465.

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We have compared mouse embryos of three heterozygous, congenic genotypes (with high, medium and low levels of oocyte-coded glucose phosphate isomerase (GPI-1) activity respectively) to test whether 1) the survival time of oocyte-coded GPI-1 activity in the early embryo is affected by its activity level in the oocyte and 2) whether embryo-coded GPI-1 is detected earlier in embryos that inherit low levels of oocyte-coded GPI-1. The oocyte-coded GPI-1 was entirely GPI-1A allozyme in the high and medium groups but was the less stable GPI-1C allozyme in the low group. We determined total GPI-1 activity and the ratio of different GPI-1 allozymes in early embryos and calculated the activity of oocyte-coded and embryo-coded GPI-1. In all three groups, the oocyte-coded enzyme activity remained at a more or less constant level for the first 21 1/2 days. Some oocyte-coded GPI-1 remained in 4 1/2 day embryos from the high and medium groups but was gone by 5 1/2 days. Very little remained in 4 1/2 day embryos that inherited low levels of a less stable form of the enzyme (GPI-1C allozyme). Despite a 4- to 5-fold difference in initial oocyte-coded GPI-1 activity, no differences were seen among the three genotypically distinct groups of embryos in the time of activation of the embryonic Gpi-1s genes. The embryo-coded GPI-1 was first detectable in 3 1/2 day compacted morulae in all three groups. The level of oocyte-coded GPI-1, in the high group, when embryo-coded GPI-1 was first detected was higher than the level in the low group at any stage prior to detection of embryo-coded GPI-1.(ABSTRACT TRUNCATED AT 250 WORDS)

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38

Wiame, Elsa, Pedro Lamosa, Helena Santos, and Emile Van Schaftingen. "Identification of glucoselysine-6-phosphate deglycase, an enzyme involved in the metabolism of the fructation product glucoselysine." Biochemical Journal 392, no. 2 (November 22, 2005): 263–69. http://dx.doi.org/10.1042/bj20051183.

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The metabolism of the glycation product fructose-ϵ-lysine in Escherichia coli involves its ATP-dependent phosphorylation by a specific kinase (FrlD), followed by the conversion of fructoselysine 6-phosphate into glucose 6-phosphate and lysine by fructoselysine-6-phosphate deglycase (FrlB), which is distantly related to the isomerase domain of glucosamine-6-phosphate synthase. As shown in the present work, several bacterial operons comprise: (1) a homologue of fructoselysine-6-phosphate deglycase; (2) a second homologue of the isomerase domain of glucosamine-6-phosphate synthase, more closely related to it; and (3) components of a novel phosphotransferase system, but no FrlD homologue. The FrlB homologue (GfrF) and the closer glucosamine-6-phosphate synthase homologue (GfrE) encoded by an Enterococcus faecium operon were expressed in E. coli and purified. Similar to FrlB, GfrF catalysed the reversible conversion of fructoselysine 6-phosphate into glucose 6-phosphate and lysine. When incubated with fructose 6-phosphate and elevated concentrations of lysine, GfrE catalysed the formation of a compound identified as 2-ϵ-lysino-2-deoxy-6-phospho-glucose (glucoselysine 6-phosphate) by NMR. GfrE also catalysed the reciprocal conversion, i.e. the formation of fructose 6-phosphate (but not glucose 6-phosphate) from glucoselysine 6-phosphate. The equilibrium constant of this reaction (0.8 M) suggests that the enzyme serves to degrade glucoselysine 6-phosphate. In conclusion, GfrF and GfrE serve to metabolize glycation products formed from lysine and glucose (fructoselysine) or fructose (glucoselysine), via their 6-phospho derivatives. The latter are presumably formed by the putative phosphotransferase system encoded by gfrA–gfrD. The designation gfr (glycation and fructation product degradation) is proposed for this operon. This is the first description of an enzyme participating in the metabolism of fructation products.

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39

Rodriguez-Rodriguez, Patricia, Emilio Fernandez, and Juan P. Bolaños. "Underestimation of the Pentose–Phosphate Pathway in Intact Primary Neurons as Revealed by Metabolic Flux Analysis." Journal of Cerebral Blood Flow & Metabolism 33, no. 12 (September 25, 2013): 1843–45. http://dx.doi.org/10.1038/jcbfm.2013.168.

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The rates of glucose oxidized at glycolysis and pentose–phosphate pathway (PPP) in neurons are controversial. Using [3-3H]-, [1-14C]-, and [6-14C]glucose to estimate fluxes through these pathways in resting, intact rat cortical primary neurons, we found that the rate of glucose oxidized through PPP was, apparently, ∼14% of total glucose metabolized. However, inhibition of PPP rate-limiting step, glucose-6-phosphate (G6P) dehydrogenase, increased approximately twofold the glycolytic rate; and, knockdown of phosphoglucose isomerase increased ∼1.8-fold the PPP rate. Thus, in neurons, a considerable fraction of fructose-6-phosphate returning from the PPP contributes to the G6P pool that re-enters PPP, largely underestimating its flux.

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40

Hirota, Tomoya, Hiroto Tsuboi, Mana Iizuka-Koga, Hiroyuki Takahashi, Hiromitsu Asashima, Masahiro Yokosawa, Yuya Kondo, et al. "Suppression of glucose-6-phosphate-isomerase induced arthritis by oral administration of transgenic rice seeds expressing altered peptide ligands of glucose-6-phosphate-isomerase." Modern Rheumatology 27, no. 3 (February 1, 2017): 457–65. http://dx.doi.org/10.1080/14397595.2016.1218598.

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41

Gooding, R. H., and B. M. Rolseth. "Genetics of Glossina morsitans morsitans (Diptera: Glossinidae). XIV. Map locations of the loci for phosphoglucomutase and glucose-6-phosphate isomerase." Genome 35, no. 4 (August 1, 1992): 699–701. http://dx.doi.org/10.1139/g92-106.

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The locus for phosphoglucomutase (Pgm) was mapped at less than 1.2 recombination units from the locus for arginine phophokinase (Apk) in linkage group I, the X chromosome. Linkage group III loci were mapped in the order sabr (long scutellar apical bristles in females), Mdh (malate dehydrogenase), and Pgi (glucose-6-phosphate isomerase). The loci sabr and Mdh were separated by 39.3 ± 4.6 recombination units, and Mdh and Pgi were separated by 45.5 ± 4.7 recombination units. Intrachromosomal recombination was rare or did not occur in males. Previously published recombination distances are summarized as a linkage map for the 16 loci that have been mapped in Glossina morsitans morsitans.Key words: tsetse, linkage map, phosphoglucomutase, glucose-6-phosphate isomerase.

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42

Hansen, Thomas, Margitta Oehlmann, and Peter Schönheit. "Novel Type of Glucose-6-Phosphate Isomerase in the Hyperthermophilic Archaeon Pyrococcus furiosus." Journal of Bacteriology 183, no. 11 (June 1, 2001): 3428–35. http://dx.doi.org/10.1128/jb.183.11.3428-3435.2001.

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ABSTRACT Glucose-6-phosphate isomerase (phosphoglucose isomerase [PGI]) (EC 5.3.1.9 ) from the hyperthermophilic archaeon Pyrococcus furiosus was purified 500-fold to homogeneity. The enzyme had an apparent molecular mass of 43 kDa and was composed of a single type of subunit of 23 kDa indicating a homodimeric (α2) structure. Kinetic constants of the enzyme were determined at the optimal pH 7 and at 80°C. Rate dependence on both substrates followed Michaelis-Menten kinetics. The apparent Km values for glucose-6-phosphate and fructose-6-phosphate were 8.7 and 1.0 mM, respectively, and the corresponding apparentV max values were 800 and 130 U/mg. The enzyme had a temperature optimum of 96°C and showed a significant thermostability up to 100°C, which is in accordance with its physiological function under hyperthermophilic conditions. Based on the N-terminal amino acid sequence of the subunit, a single open reading frame (ORF; Pf_209264) was identified in the genome of P. furiosus. The ORF was characterized by functional overexpression in Escherichia coli as a gene, pgi, encoding glucose-6-phosphate isomerase. The recombinant PGI was purified and showed molecular and kinetic properties almost identical to those of the native PGI purified from P. furiosus. The deduced amino acid sequence of P. furiosus PGI did not reveal significant similarity to the conserved PGI superfamily of eubacteria and eucarya. This is the first description of an archaeal PGI, which represents a novel type of PGI.

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43

William, M. D. H. M., and Abdul Mujeeb-Kazi. "Rapid detection of 1B, 1BL/1RS heterozygotes in the development of homozygous 1BL/1RS translocation stocks of Triticum turgidum (2n = 4x = 28)." Genome 36, no. 6 (December 1, 1993): 1088–91. http://dx.doi.org/10.1139/g93-144.

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A biochemical marker was utilized to facilitate detection of chromosome 1B, 1BL/1RS translocation heterozygote plants in segregating backcross progenies during the development of 1BL/1RS homozygous lines in several Triticum turgidum L. cultivars (2n = 4x = 28; AABB). Isoelectric focussing of glucose phosphate isomerase (GPI) on either pH 3.5–9.5 or 5.5–8.5 polyacrylamide gels facilitated the detection of 1B, 1BL/1RS translocation heterozygotes from the homozygous 1B or 1BL/1RS derivatives during each backcross of the heterozygote to the respective recurrent parent. The biochemical diagnostic procedure complements the more time consuming and cumbersome chromosome banding technique. This GPI diagnostic in durum 1BL/1RS development is also swifter than a similar stocks development in T. aestivum where both GPI and acid PAGE are essential.Key words: Triticum turgidum, glucose phosphate isomerase, 1BL/1RS translocation, isoelectric focusing.

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44

Rubino, David B. "INHERITANCE OF DIAPHORASE AND GLUCOSE-6-PHOSPHATE ISOMERASE IN EUSTOMA GRANDIFLORUM." HortScience 27, no. 6 (June 1992): 680a—680. http://dx.doi.org/10.21273/hortsci.27.6.680a.

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Segregating progenies from controlled pollinations of Eustoma grandiflorum Griseb. were investigated to determine the inheritance of diaphorase (DIA) and glucoses-phosphate isomerase (GPI) isozymes. Phenotypic data supported the hypotheses that DIA1 is tetrameric and is controlled by a single locus with two alleles (Dia1-1 and Dia1-2) and that GPI1 is dimeric and also is controlled by a single locus with two alleles (Gpi1-1 and Gpi1-2). Examination of isozyme phenotypes for over 70 cultivars of E. grandiflorum revealed polymorphism for DIA1 and GPI1. These isozymes may be useful for marker-assisted selection and cultivar identification.

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45

Rubino, David B. "Inheritance of Esterase, Diaphorase, and Glucose-6-phosphate Isomerase in Lisianthus." HortScience 28, no. 6 (June 1993): 661–63. http://dx.doi.org/10.21273/hortsci.28.6.661.

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Segregating lisianthus [Eustoma grandiflorum (Griseb.) Shinn.] progeny were evaluated to determine the inheritance of esterase (EST), diaphorase (DIA), and glucose-6-phosphate isomerase (GPI) isozymes. Phenotypic data supported the hypotheses that EST is monomeric and controlled by one locus (Est1) with at least three alleles, DIA is tetrameric and controlled by one locus (Dia2) with at least two alleles, and GPI is controlled by one locus (Gpil) with at least two alleles. The structure of the GPI isozyme could not be inferred from banding patterns. Joint segregation analyses indicated that the three loci segregate independently. These three isozymes are the first simply inherited, unlinked biochemical markers identified in lisianthus. These marker loci will be useful for genetic studies, breeding, and germplasm characterization.

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46

Tanabe, Yuichi, Tokiyoshi Omi, and Katuaki Ota. "Genetic variants of glucose phosphate isomerase (E.C. 5.3.1.9) in canine erythrocytes*." Animal Blood Groups and Biochemical Genetics 8, no. 1 (April 24, 2009): 191–95. http://dx.doi.org/10.1111/j.1365-2052.1977.tb01646.x.

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47

NAKAMURA, Takashi, Harumoto KAWAGUCHI, and Jun IMOSE. "Identification of Eimeria brunetti using glucose phosphate isomerase and lactate dehydrogenase." Japanese Journal of Veterinary Science 52, no. 4 (1990): 859–60. http://dx.doi.org/10.1292/jvms1939.52.859.

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48

GOMEZ-GALLEGO, FELIX, AMANDO GARRIDO-PERTIERRA, and JOSE M. BAUTISTA. "Protein disulphide isomerase assisted folding of human glucose-6-phosphate dehydrogenase." Biochemical Society Transactions 23, no. 1 (February 1, 1995): 82S. http://dx.doi.org/10.1042/bst023082s.

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49

Xu, Weiming, and Ernest Beutler. "An Exonic Polymorphism in the Human Glucose Phosphate Isomerase (GPI) Gene." Blood Cells, Molecules, and Diseases 23, no. 3 (December 1997): 377–79. http://dx.doi.org/10.1006/bcmd.1997.0154.

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50

Walker, James I. H., Michael J. Morgan, and Pelin Faik. "Structure and Organization of the Human Glucose Phosphate Isomerase Gene (GPI)." Genomics 29, no. 1 (September 1995): 261–65. http://dx.doi.org/10.1006/geno.1995.1241.

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