Untersuchungen über Proteinstruktur und Enzymaktivität, I. Darstellung und Eigenschaften kristallisierter Glucose-6-phosphat-Dehydrogenase aus<i>Candida utilis</i>

Domagk, Götz F.; Chilla, R; Domschke, Wolfram; Engel, Heinz Jürgen; Sørensen, N. Kr.

doi:10.1515/bchm2.1969.350.1.626

Cited by 32 publications

(7 citation statements)

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“…Since M, of glucose-6-phosphate dehydrogenase is reported to be 104000 [20] it is unlikely that the enzyme penetrates through intact outer membranes. To ascertain this, glucose-6-phosphate dehydrogenase and Ficoll 400 (Mr, 400000, Pharmacia, Uppsala) were mixed and the penetration experiment was carried out as above.…”

Section: Penetration Assaymentioning

confidence: 99%

A small diffusion pore in the outer membrane of Pseudomonas aeruginosa

Yoneyama

Nakae

1986

Eur J Biochem

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The permeability properties of the outer membrane of Pseudomonas aeruginosa were re-examined, since the reported conclusions are conflicting [Decad, M. G. and Nikaido, H. (1976) J. Bacteriol. 128, 325-336; Caulcott, C. A., Brown, M. R. W. and Gonda, I. (1984) FEMS Microbiol. Lett. 21, 119-1231, On the basis of the experimental evidence to be described below we conclude that the exclusion limit of the outer membrane of P. aeruginosa is smaller than the size of uncharged disaccharides but larger than the size of hexose. This conclusion is based on the following evidence. (a) Penetration of monosaccharides into the expanded periplasm was large and that of disaccharides was small, after the cells were plasmolyzed with 600 mosM NaCl. (b) A significant amount of protein was released after osmotic down-shock of cells treated with the hypertonic monosaccharides but not of cells treated with the hypertonic saccharides larger than disaccharides. (c) Centrifuged pellets of cells treated with hypertonic di, tri and tetrasaccharides weighed about 15 -20% less than that of cells treated with the isotonic monosaccharide, suggesting that the osmotic pressure was exerted on the outer membrane causing dehydration and shrinking of the cells. By contrast, cells treated with the hypertonic pentose and hexoses weighed about 0.1% and 6% less, respectively, than cells treated with the isotonic saccharide, suggesting that pentose diffused through the outer membrane freely.The outer membrane of gram-negative bacteria prevents the access of hydrophobic and large hydrophilic compounds into the cells [l -31. This membrane contains a set of poreforming proteins (porins) through which small hydrophilic nutrients and metabolic wastes diffuse [4, 51. The sieve property of the porin pores in various gram-negatives may, in terms of pore size, be roughly divided into two groups. (a) The porins having small pores showing an apparent exclusion limit close to the size of uncharged saccharides of M , about 700. These are the porins from Escherichia coli [5], Salmonella typhimurium [4], Proteus mirubilis [6], Enterobacter [6] and Yersinia pestis [7]. (b) The porins having large pores with an exclusion limit similar to the size of uncharged polysaccharides with M , of several thousands. This group includes the porins from Pseudomonas ueruginosa [2, 81, Paracoccus denitrificans [9], Anabaena variabilis [lo] and Chlamydia trachomatis [ll].The clinical relevance of P. aeruginosa is the high incidence of opportunistic infections and its resistance to a wide range of antibiotics [12]. This intrinsic drug resistance of P. aeruginosa is mainly due to the diffusion barrier of the outer membrane [13 -151. However, the pore in the outer membrane of P. aeruginosa was reported to be so large that it allows the diffusion of saccharides with Mr of several thousands [2, 81. The presence of the large pore in the membrane was confirmed by in vitro reconstitution experiments [8, 16, 171. To explain this apparent discrepancy it was proposed [13,15,16,18] that the major...

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Section: Penetration Assaymentioning

confidence: 99%

A small diffusion pore in the outer membrane of Pseudomonas aeruginosa

Yoneyama

Nakae

1986

Eur J Biochem

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“…However, some inhibition of the enzyme by the free derivative had been observed (Table 2), and furthermore adenosine 5'-monophosphate has been shown to be inhibitor for this enzyme from Candida utilis (Torula yeast) [18].…”

Section: Model Studiesmentioning

confidence: 99%

The Synthesis of Three AMP‐Analogues: N⁶‐(6‐Aminohexyl)‐adenosine 5′‐Monophosphate, N⁶‐(6‐Aminohexyl)‐adenosine 2′,5′‐Bisphosphate, and N⁶‐(6‐Aminohexyl)‐adenosine 3′,5′‐Bisphosphate and Their Application as General Ligands in Biospecific Affinity Chromatography

Brodelius¹,

Larsson²,

Mosbach³

1974

European Journal of Biochemistry

101

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Phosphorylation of 6-chloropurine riboside with phosphorus oxychloride and phosphorus trichloride gave a mixture of the two isomers, 6-chloropurine-riboside 2',5'-bisphosphate and 6-chloropurine-riboside 3',5'-bisphosphate. Reaction with Iy6-diaminohexane followed by resolution of the isomeric mixture on a Dowex 1-X2 column yielded N6-(6-aminohexyl)-adenosine 2',5'-bisphosphate and N6-(6-aminohexyl)-adenosine 3',5'-bisphosphate.The inhibition of several NADP+-dependent and NAD+-dependent dehydrogenases by N6-(6-aminohexyl)-adenosine 2',5'-bisphosphate, N6-(6-aminohexyl)-adenosine 3',5'-bisphosphate and N6-(6-aminohexyl)-adenosine 5'-monophosphate was examined.These three AMP-analogues were attached to Sepharose 4B by the cyanogen bromide method and the binding of several NAD(P)+-dependent enzymes were investigated. NADP+-dependent enzymes were bound to Sepharose substituted with N6-(6-aminohexyl)-adenosine 2',5'-bisphosphate, whereas NAD+-dependent enzymes were not bound under the same conditions. Conversely, when N6-(6-aminohexy1)-adenosine 5'-monophosphate was used as the immobilised ligand only the NAD+-dependent enzymes were bound, as well as glucose-6-phosphate dehydrogenase showing weak affinity. These observations strongly suggest that these two immobilised analogues represent true biospecific and group-specific adsorbents. The enzymes were eluted with their complementary nucleotides, NAD(H) and NADP(H). These techniques were utilised to purify several NADPf-dependent enzymes from a crude Candida utilis extract by chromatography on the new biospecific adsorbent.The development during the last three years of biospecific adsorbents of the "general ligand" type to be used in affinity chromatography has proven most valuable [I-51. Ligands of this nature have, as the name implies, affinity for large groups of enzymes and therefore great versatility. The separation or purification of one particular enzyme can subsequently be achieved by application of biospecific elution.Enzymes.

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“…This approach led to the demonstration of a critical lysine residue in Candida utilis 6-phosphogluconate dehydrogenase (Rippa et al, 1967;Rippa and Pontremoli, 1969) and in rabbit muscle aldolase (Shapiro et al, 1968). The present investigation was therefore initiated to test the suitability of pyridoxal 5'-phosphate as a sitespecific protein reagent for the catalytically critical lysine residue postulated for rabbit muscle phosphoglucose isomerase.1 Numerous other reports have now appeared in the literature which confirm the usefulness of pyridoxal 5 '-phosphate as a tool for the identification of lysine residues (e.g., Kaldor and Weinbach, 1966;Anderson et al, 1966; Marcus and Hubert, 1968;Ronchi et al, 1969;Benesch et al, 1969;Domagk et al, 1969;Uyeda, 1969;Johnson and Deal, 1970;Piszkiewicz et a!., 1970;Porcina et a!., 1971;Shematek and Arfin, 1971). Moreover, while testing the effect of pyridoxal 5 '-phosphate on various glycolytic enzymes, Domschke and Domagk (1969) have also observed inhibition of yeast phosphoglucose isomerase.…”

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confidence: 92%

Pyridoxal 5'-phosphate as a site-specific protein reagent for a catalytically critical lysine residue in rabbit muscle phosphoglucose isomerase

Schnackerz¹,

Noltmann²

1971

Biochemistry

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INHIBITION OF PHOSPHOGLUCOSEISOMERASE BY PYRIDOXAL PHOSPHATE 3-Hydroxy-5 '-methyl-4,5 '-retro-5 'apo-/3-caroten-5'-one or 3-hydroxy-4,5 '-re/ro-5 '-apo-ßcaroten-5'-one 2-(4-Hydroxy-3-methyl-2-butenyl> 7',8',11',12 '-tetrahydroe,carotene Tangeraxanthin Nonaprenoxanthin 2,2'-Bis(4-hydroxy-3-methyl-2-butenyl>e,e-carotene :h2oh Decaprenoxanthin 2-[4-Hydroxy-3-(hydroxymethyl>2butenyl]-2'-(3-methyl-2-butenyl)ß, (3-carotene 2'-(4-Hydroxy-3-methyl-2-butenyl)-2-(3-methyl-2-butenyl> 3 ',4 'didehydro-1',2'-dihydro-d,V" caroten-l'-ol 2,2 '-Bis( 3-hydroxy-3-methylbutyl> 3,4,3' ,4 '-tetradehydro-1,2,1 ',2'tetrahydro-/', -carotene-1,1 '-diol C.p. 450 C.p. 473

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Untersuchungen über Proteinstruktur und Enzymaktivität, I. Darstellung und Eigenschaften kristallisierter Glucose-6-phosphat-Dehydrogenase ausCandida utilis

Cited by 32 publications

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A small diffusion pore in the outer membrane of Pseudomonas aeruginosa

A small diffusion pore in the outer membrane of Pseudomonas aeruginosa

Pyridoxal 5'-phosphate as a site-specific protein reagent for a catalytically critical lysine residue in rabbit muscle phosphoglucose isomerase

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Untersuchungen über Proteinstruktur und Enzymaktivität, I. Darstellung und Eigenschaften kristallisierter Glucose-6-phosphat-Dehydrogenase ausCandida utilis

Cited by 32 publications

References 0 publications

A small diffusion pore in the outer membrane of Pseudomonas aeruginosa

A small diffusion pore in the outer membrane of Pseudomonas aeruginosa

The Synthesis of Three AMP‐Analogues: N6‐(6‐Aminohexyl)‐adenosine 5′‐Monophosphate, N6‐(6‐Aminohexyl)‐adenosine 2′,5′‐Bisphosphate, and N6‐(6‐Aminohexyl)‐adenosine 3′,5′‐Bisphosphate and Their Application as General Ligands in Biospecific Affinity Chromatography

Pyridoxal 5'-phosphate as a site-specific protein reagent for a catalytically critical lysine residue in rabbit muscle phosphoglucose isomerase

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