Isolation and characterization of the phosphoglucose isomerase gene from Escherichia coli

Froman, Byron E.; Tait, Robert C.; Gottlieb, L. D.

doi:10.1007/bf00330951

Cited by 55 publications

(30 citation statements)

References 38 publications

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“…6. Phosphoglucose isomerase from Z. mobilis exhibited 43% sequence identity to the E. coli phosphoglucose isomerase (14). The results of comparisons of the amino acid sequence of the Z. mobilis pgi product with the amino acid sequences of phosphoglucose isomerase enzymes from Kluyveromyces lactis (37), Clarkia unguiculata (32), Trypanosoma brucei (23), S. cerevisiae (33), and pigs (4) are shown in Table 2.…”

Section: Resultsmentioning

confidence: 99%

Cloning, characterization, and nucleotide sequence analysis of a Zymomonas mobilis phosphoglucose isomerase gene that is subject to carbon source-dependent regulation

1991

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Section: Resultsmentioning

confidence: 99%

Cloning, characterization, and nucleotide sequence analysis of a Zymomonas mobilis phosphoglucose isomerase gene that is subject to carbon source-dependent regulation

1991

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“…The apparent K m values and V max values were determined at 80°C in a discontinuous assay in the direction of F-6-P formation and G-6-P formation. (14), pig (7), rabbit (20), and human (12) type of PGI, probably forming a separate branch of PGI evolution.…”

Section: Discussionmentioning

confidence: 99%

Novel Type of Glucose-6-Phosphate Isomerase in the Hyperthermophilic Archaeon Pyrococcus furiosus

2001

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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 (␣ 2 ) 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 K m values for glucose-6-phosphate and fructose-6-phosphate were 8.7 and 1.0 mM, respectively, and the corresponding apparent V 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.Glucose-6-phosphate isomerase, or phosphoglucose isomerase (PGI) (EC 5.3.1.9), catalyzes the reversible isomerization of glucose-6-phosphate (G-6-P) to fructose-6-phosphate (F-6-P). PGI plays a central role in the sugar metabolism of members of the domains Bacteria and Eucarya, both in glycolysis via the Embden-Meyerhof (EM) pathway and in gluconeogenesis, where the enzyme operates in the reverse direction (29,31).In the Archaea domain, PGI was first demonstrated to be part of the gluconeogenetic pathways in various species of lithoautotrophic methanogens and in the sulfur-reducing lithoautotrophic Thermoproteus species (15,35,43,51). In recent years, the pathways of sugar degradation have been studied in various hyperthermophilic archaea (44), such as the Euryarchaeota Pyrococcus furiosus and Thermococcus celer and the Crenarchaeota Desulfurococcus amylolyticus and Thermoproteus tenax. These hyperthermophiles have been found to degrade glucose, maltose, cellobiose, and starch via modified versions of the EM pathway. The modified pathways differ from the conventional EM pathway by the involvement of novel kinases, such as ADP-dependent hexokinase and ADP-dependent 6-phosphofructokinase (6-PFK), in P. furiosus and T. celer and of unusual enzymes of glyceraldehyde-3-phosphate oxidation, such as glyceraldehyde:ferredoxin oxidoreductase, inP.furiosus,T.celer,andD.amylolyticusandnonphosphorylating NAD ϩ -reducing glyceraldehyde 3-phosphate dehydrogenase in T. tenax (5,11,17,22,38,42). However, all these modified EM pathways involve the activity...

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“…1). Fructose 1,6-bisphosphatase (EC 3.1.3.11) catalyzes the second irreversible step in gluconeogenesis producing fructose-6-P that is further converted into glucose-6-P by phosphoglucose isomerase Pgi (52). Two fructose 1,6-bisphosphatases have been characterized in E. coli, namely Fbp and GlpX, both members of the inositol polyphosphate 1-phosphatase-like superfamily (53,54).…”

Section: Metabolites Hydrolyzed By the E Coli Hads-e Colimentioning

confidence: 99%

Genome-wide Analysis of Substrate Specificities of the Escherichia coli Haloacid Dehalogenase-like Phosphatase Family

Kuznetsova

Proudfoot

González

et al. 2006

Journal of Biological Chemistry

266

323

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Most enzymes form families of paralogs whose members are related by sequence and catalyze similar reactions but have evolved specific biological functions. Comprehensive determination of the substrate specificities and selectivities of all metabolic enzymes in an organism is an essential step toward understanding the relationship between the proteome and the metabolome. By the most recent estimate, Escherichia coli possesses at least 1186 metabolic enzymes and 1005 metabolites (1). The most common functional group in the metabolome is phosphate; 35-40% of the metabolites contain a phosphate group (2). The pool of phosphorylated metabolites is controlled by the activity of diverse kinases and phosphatases, of which there are hundreds in the E. coli genome.

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Isolation and characterization of the phosphoglucose isomerase gene from Escherichia coli

Cited by 55 publications

References 38 publications

Cloning, characterization, and nucleotide sequence analysis of a Zymomonas mobilis phosphoglucose isomerase gene that is subject to carbon source-dependent regulation

Cloning, characterization, and nucleotide sequence analysis of a Zymomonas mobilis phosphoglucose isomerase gene that is subject to carbon source-dependent regulation

Novel Type of Glucose-6-Phosphate Isomerase in the Hyperthermophilic Archaeon Pyrococcus furiosus

Genome-wide Analysis of Substrate Specificities of the Escherichia coli Haloacid Dehalogenase-like Phosphatase Family

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