Phosphomannoisomerase, an SH-Dependent Metal-Enzyme Complex

Bruns, Friedrich; Noltmann, Ernst A.

doi:10.1038/1811467a0

Cited by 13 publications

(6 citation statements)

References 6 publications

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“…The natural enzyme has not been purified in sufficient quantities from other species to enable unequivocal identification of the metal ion. Porcine PMI has previously been 1000 100 I I I | I I I I I I shown to be sensitive to chelators (Bruns et aL, 1958). We have shown that PMI from all four species can be irreversibly inactivated by metal chelators such as EDTA, 1,10-phenanthroline, and dithiothreitol, which points toward a transition metal being in the active site.…”

Section: Resultsmentioning

confidence: 78%

“…Studies have shown that over 25% of HIV-infected patients acquire visceral mycoses, and up to 20% of the deaths in these patients were caused by the mycoses (Manfredi et al, 1993). Phosphomannose isomerase activity has been detected in mammalian tissues such as porcine erythrocytes and rat liver (Bruns et al, 1958). The requirement for PMI activity in mammalian cells is not so clear.…”

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confidence: 99%

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Purification and characterization of fungal and mammalian phosphomannose isomerases

Proudfoot¹,

Payton²,

Wells³

1994

J Protein Chem

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Phosphomannose isomerase (PMI) is essential for the production of yeast cell walls. An inhibitor which inhibits the fungal enzyme without altering the activity of the mammalian enzyme would be a potential fungicidal agent, increasingly important in view of the increasing mortality from visceral mycoses in immunosuppressed patients. We have purified human, porcine, and Candida albicans enzymes 29,000-fold to homogeneity, and characterized their physical properties, as well as their kinetic parameters, inhibition constants, and pH dependences. Surprisingly, in view of the large differences between Pseudomonas aerugenosa and Saccharomyces cerevisiae PMI, the human and C. albicans enzymes are almost identical. We suggest therefore that species-selective inhibition of the fungal rather than mammalian enzyme may require molecules which bind away from the substrate binding pocket of the enzyme.

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Section: Resultsmentioning

confidence: 78%

mentioning

confidence: 99%

Purification and characterization of fungal and mammalian phosphomannose isomerases

Proudfoot¹,

Payton²,

Wells³

1994

J Protein Chem

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“…Colajacomo, Missale, Vergnano & Luzzatto (1957) also observed non-oxidative heptulose formation in sarcoma 181 ascites and Ehrlich solid carcinoma form. Measurements have been made of transketolase in erythrocytes and in different regions of the brain from normal and thiamine-deficient rats (Brin, 1967;Dreyfus, 1967), and the activity of ribose 5-phosphate isomerase has been reported for erythrocytes and a number of other tissues such as heart, skeletal muscle, liver and kidney (Bruns, Noltmann & Vahlhaus, 1958). The presence of a highly active ribulose 5-phosphate 3-epimerase from muscle and tumour cells and its almost complete absence from erythrocytes was observed by Dickens & Williamson (1956).…”

Section: Enzyme Activitie8 In Tis8uesmentioning

confidence: 99%

The pentose phosphate pathway of glucose metabolism. Measurement of the non-oxidative reactions of the cycle

Novello

McLean

1968

Biochemical Journal

132

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Methods for the quantitative determination of ribose 5-phosphate isomerase, ribulose 5-phosphate 3-epimerase, transketolase and transaldolase in tissue extracts are described. The determinations depend on the measurement of glyceraldehyde 3-phosphate by using the coupled system triose phosphate isomerase, alpha-glycero-phosphate dehydrogenase and NADH. By using additional purified enzymes transketolase, ribose 5-phosphate isomerase and ribulose 5-phosphate epimerase conditions could be arranged so that each enzyme in turn was made rate-limiting in the overall system. Transaldolase was measured with fructose 6-phosphate and erythrose 4-phosphate as substrates, and again glyceraldehyde 3-phosphate was measured by using the same coupled system. Measurements of the activities of the non-oxidative reactions of the pentose phosphate pathway were made in a variety of tissues and the values compared with those of the two oxidative steps catalysed by glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase.

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“…Except for hexokinase, these enzymes are located exclusively in the non-sedimentable portion of the organism. Rigid exclusion of formed blood elements, which are known to contain adenosine triphosphatase (Caffrey, Tremblay, Gabrio & Huennekens, 1956) and hexose monophosphate oxidative-cycle enzymes (Bruns, Noltmann & Vahlhaus, 1958), has shown further that the enzymes in spirochaetal homogenates are predominantly glycolytic. Indeed, the suitability of phosphorylated sugars as substrates in the DPN+reduction system indicates the ability of these spirochaetes to participate in conventional reactions of glycolysis.…”

Section: Discussionmentioning

confidence: 99%

Carbohydrate metabolism in Spirochaeta recurrentis. 2. Enzymes associated with disintegrated cells and extracts of spirochaetes

Smith

1960

Biochemical Journal

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In the preceding paper (Fulton & Smith, 1960) it was shown that the only pathway of glucose catabolism in Spirochaeta recurrentis is by glycolysis to lactic acid. In this paper the results of experiments are described which show the presence of the enzymes of the Embden-Meyerhof route in disintegrated spirochaetes and cell-free extracts. EXPERIMENTAL The following abbreviations are used in this paper: DPN+, DPNH, oxidized and reduced diphosphopyridine nucleotide; TPN+, TPNH, oxidized and reduced triphosphopyridine nucleotide; ATP, ADP, adenosine triand di-phosphate; EDTA, sodium ethylenediaminetetraacetate.

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Phosphomannoisomerase, an SH-Dependent Metal-Enzyme Complex

Cited by 13 publications

References 6 publications

Purification and characterization of fungal and mammalian phosphomannose isomerases

Purification and characterization of fungal and mammalian phosphomannose isomerases

The pentose phosphate pathway of glucose metabolism. Measurement of the non-oxidative reactions of the cycle

Carbohydrate metabolism in Spirochaeta recurrentis. 2. Enzymes associated with disintegrated cells and extracts of spirochaetes

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