Results 191 to 200 of about 30,288 (231)
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The biosynthesis of guanosine diphosphate mannose and phosphomannan by Hansanula holstii
Biochimica Et Biophysica Acta, 1963The biosynthesis of phosphomannan by cultures of Hansenula holstii NRRL Y-2448 has been demonstrated to proceed from glucose with all carbons remaining intact. Enzymes were found in cell-free extracts capable of converting glucose to guanosine diphosphate mannose via mannose 1-phosphate.
R G Hansen, R K Bretthauer
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Inositol hexaphosphate guanosine diphosphate phosphotransferase from Phaseolus aureus
Phytochemistry, 1975 Inositol hexaphosphate guanosine diphosphate phosphotransferase which transfers phosphate from inositol hexaphosphate to guanosine diphosphate, synthesizing guanosine triphosphate, has been isolated from germinating mung bean.
B B Biswas
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Guanosine diphosphate d-glucose glucohydrolase
Archives of Biochemistry and Biophysics, 1966Abstract A new enzyme has been found in yeast, which catalyzes the hydrolysis of guanosine diphosphate glucose to guanosine diphosphate and glucose. The enzyme was purified about 130-fold and its kinetic properties were studied. The enzymic activity seems to be strictly specific for guanosine diphosphate glucose, with a Km of 0.23 m m . The enzyme is
S, Sonnino, H, Carminatti, E, Cabib
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Biochimica et Biophysica Acta (BBA) - General Subjects, 1966
Abstract The control of the synthesis of GDP- d -mannose and GDP- l -fucose has been studied in various classes of bacteria. In those species which contain l -fucose but no d -mannose in their polysaccharides, GDP- l -fucose inhibits both GDP- d -mannose pyrophosphorylase (GTP: α- d -mannose-1-phosphate guanylyltransferase, EC 2.7.7.13) and GDP- d -
R H, Kornfeld, V, Ginsburg
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Abstract The control of the synthesis of GDP- d -mannose and GDP- l -fucose has been studied in various classes of bacteria. In those species which contain l -fucose but no d -mannose in their polysaccharides, GDP- l -fucose inhibits both GDP- d -mannose pyrophosphorylase (GTP: α- d -mannose-1-phosphate guanylyltransferase, EC 2.7.7.13) and GDP- d -
R H, Kornfeld, V, Ginsburg
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Is Guanosine Diphosphate-D-Glucose a Precursor of Cellulose ?
Nature, 1970PARTICULATE enzyme preparations from bacteria1 and plants2,3 have been reported to catalyse the biosynthesis of high molecular weight β-1,4-linked glucan, chiefly cellulose, from either UDP-glucose or GDP-glucose. Partial hydrolysis of the polysaccharide formed from UDP-glucose, however, indicates the presence of β-1,3-linked glucose moieties4,5 ...
C L, Villemez, J S, Heller
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The Journal of Biochemistry, 1980
A radioimmunoassay for guanosine-5'-diphosphate-3'-diphosphate (ppGpp) and adenosine-5'-triphosphate-3'-diphosphate (pppApp) has been developed. The assay method is based on competition of an unlabeled highly phosphorylated nucleotide with 3H-labeled highly phosphorylated nucleotide for binding sites on a specific antibody.
Y, Hamagishi, T, Oki, H, Tone, T, Inui
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A radioimmunoassay for guanosine-5'-diphosphate-3'-diphosphate (ppGpp) and adenosine-5'-triphosphate-3'-diphosphate (pppApp) has been developed. The assay method is based on competition of an unlabeled highly phosphorylated nucleotide with 3H-labeled highly phosphorylated nucleotide for binding sites on a specific antibody.
Y, Hamagishi, T, Oki, H, Tone, T, Inui
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Analytical Biochemistry, 1982
Abstract A method is described for the rapid analysis of the nucleotides, guanosine 5′-diphosphate-3′-diphosphate (ppGpp) and guanosine 5′-triphosphate-3′-diphosphate (pppGpp), by high-performance liquid chromatography. It has been found that the inclusion of magnesium acetate in the potassium phosphate buffer facilitates elution of these highly ...
M, Fischer, T P, Zimmerman, S A, Short
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Abstract A method is described for the rapid analysis of the nucleotides, guanosine 5′-diphosphate-3′-diphosphate (ppGpp) and guanosine 5′-triphosphate-3′-diphosphate (pppGpp), by high-performance liquid chromatography. It has been found that the inclusion of magnesium acetate in the potassium phosphate buffer facilitates elution of these highly ...
M, Fischer, T P, Zimmerman, S A, Short
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Synthesis of guanosine 5′-diphosphate, 3′-diphosphate in spot mutants of Escherichia coli
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1977The synthesis of ppGpp in spoT- mutants of Escherichia coli has been invesitgated. In these mutants the first-order rate constant for ppGpp breakdown is low, and pppGpp is barely detectable. It is shown that the rate of pppGpp, and hence ppGpp, synthesis is strongly reduced compared with that observed in spot+ strains.
DEBOER, HA +4 more
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Presence of Guanosine 5'-Diphosphate 3'-Diphosphate in Bacillus subtilis Vegetative Cells
The Journal of Biochemistry, 1981Extracts of Bacillus subtilis vegetative cells with 2 M formic acid contained a large amount of a hyperphosphorylated nucleotide ("spot 4" nucleotide). The compound always comigrated with authentic guanosine 5'-diphosphate 3'-diphosphate (ppGpp) on two-dimensional polyethyleneimine (PEI)-cellulose thin-layer chromatography performed with three ...
K, Ikehara, H, Ando, Y, Takada, K, Sugae
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A convenient enzymic synthesis of guanosine diphosphate-[14C]mannose
Analytical Biochemistry, 1982Abstract A cell-free extract from baker's yeast supplemented with hexokinase, GTP, 3-phosphoglyceric acid, and glucose 1,6-diphosphate converts [14C]mannose to GDP-[14C]mannose in 55–60% yield. Addition of EDTA to the reaction mixture prevents the formation of glycolytic products by inactivating phosphomannose isomerase.
T J, Grier, J R, Rasmussen
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