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  • 1
    Electronic Resource
    Electronic Resource
    Metabolic regulation of the glucose-6-phosphate dehydrogenase from Paracoccus denitrificans grown on glucose/nitrate (1977)
    Springer
    Archives of microbiology 112 (1977), S. 225-227 
    Details
    ISSN: 1432-072X
    Keywords: Glucose-6-phosphate dehydrogenase ; Paracoccus denitrificans ; Nicotinamide adenine dinucleotide (phosphate) ; Adenosinetriphosphate ; Phosphoenolpyruvate ; Enzyme regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Glucose-6-phosphate dehydrogenase (d-glucose-6-phosphate: NADP+ l-oxidoreductase EC 1.1.1.49) isolated from Paracoccus denitrificans grown on glucose/nitrate exhibits both NAD+-and NADP+-linked activities. Both activities have a pH optimum of pH 9.6 (Glycine/NaOH buffer) and neither demonstrates a Mg2+ requirement. Kinetics for both NAD(P)+ and glucose-6-phosphate were investigated. Phosphoenolpyruvate inhibits both activities in a competitive manner with respect to glucose-6-phosphate. ATP inhibits the NAD+-linked activity competitively with respect to glucose-6-phosphate but has no effect on the NADP+-linked activity. Neither of the two activities are inhibited by 100 μM NADH but both are inhibited by NADPH. The NAD+-linked activity is far more sensitive to inhibition by NADPH than the NADP+-linked activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00429339
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  • 2
    Electronic Resource
    Electronic Resource
    Metabolic regulation of pyruvate kinase isolated from autotrophically and heterotrophically grown Paracoccus denitrificans (1977)
    Springer
    Archives of microbiology 115 (1977), S. 67-71 
    Details
    ISSN: 1432-072X
    Keywords: Pyruvate kinase ; Paracoccus denitrificans ; Ribose-5-phosphate ; Glucose-6-phosphate ; Adenosine monophosphate ; Enzyme regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Pyruvate kinase (ATP: pyruvate phosphotransferase (EC 2.7.1.40) was partially purified from both autotrophically and heterotrophycally grown Paracoccus denitrificans. The organism grown under heterotrophic conditions contains four times more pyruvate kinase than under autotrophic conditions. The enzyme isolated from both sources exhibited sigmoidal kinetics for both phosphoenolpyruvate (PEP) and ADP. The apparent M m for ADP and PEP in the “autotrophic” enzyme were 0.63 mM ADP and 0.25 mM PEP. The effect of several low molecular weight metabolites on the pyruvate kinase activity was investigated. Ribose-5-phosphate, glucose-6-phosphate and AMP stimulated the reaction at low ADP levels; this stimulation was brought about by an alteration in the apparent K m for ADP. The pyruvate kinases differ in their response to adenine nucleotides, but both preparations seem to be under adenylate control. The results are discussed in relation to the role of pyruvate kinase as a regulatory enzyme in P. denitrificans grown under both autotrophic and heterotrophic conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00427847
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  • 3
    Electronic Resource
    Electronic Resource
    Crystallization of Escherichia coli enoyl reductase and its complex with diazaborine (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 1181-1184 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Recent work has shown that the NADH-dependent enoyl acyl carrier protein reductase from Escherichia coli is the target for diazaborine, an antibacterial agent. This enzyme has been crystallized by the hanging-drop method of vapour diffusion complexed with NAD+ and in the presence and absence of a thieno diazaborine. The crystals grown in the absence of diazaborine (form A) are in the space group P21 with unit-cell dimensions a = 74.0, b = 81.2, c = 79.0 Å and β = 92.9°, and with a tetramer in the asymmetric unit, whilst those grown in the presence of diazaborine (form B) are in the space group P6122 (or P6522) with unit-cell dimensions a = b = 80.9 and c = 328.3 Å, and with a dimer in the asymmetric unit. The structure determination of this enzyme in the presence of diazaborine will provide information on the nature of the drug binding site and contribute to a programme of rational drug design.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996005458
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  • 4
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray analysis of the glycerol-3-phosphate 1-acyltransferase from squash (Cucurbita moschata) (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 451-453 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Glycerol-3-phosphate 1-acyltransferase (E.C. 2.3.1.15; G3PAT) catalyses the incorporation of an acyl group from either acyl-acyl carrier proteins (acylACPs) or acylCoAs into the sn-1 position of glycerol 3-phosphate to yield 1-acylglycerol 3-phosphate. Crystals of squash G3PAT have been obtained by the hanging-drop method of vapour diffusion using PEG 4000 as the precipitant. These crystals are most likely to belong to space group P212121, with approximate unit-cell parameters a = 61.1, b = 65.1, c = 103.3 Å, α = β = γ = 90° and a monomer in the asymmetric unit. X-ray diffraction data to 1.9 Å resolution have been collected in-house using a MAR 345 imaging-plate system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901000257
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  • 5
    Electronic Resource
    Electronic Resource
    EPR signals in chloroplasts responding to illumination sequence of four flashes (1977)
    [s.l.] : Nature Publishing Group
    Nature 270 (1977), S. 169-171 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Manganese may be an important component of the oxygen evolving system1, but attempts to observe changes in the redox state of manganese associated with oxygen evolution have not been successful. Kinetic measurements2'3 have shown that when chloroplasts are illuminated with short intense flashes of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/270169a0
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  • 6
    Electronic Resource
    Electronic Resource
    Immunogold localization of acyl carrier protein in plants and Escherichia coli: Evidence for membrane association in plants (1988)
    Springer
    Planta 175 (1988), S. 145-152 
    Details
    ISSN: 1432-2048
    Keywords: Acyl carrier protein ; Brassica (Acyl carrier protein) ; Escherichia ; Lipid synthesis ; Persea ; Plastid (acyl carrier protein) ; Thylakoid membrane
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Immunogold labelling was used to study the distribution of acyl carrier protein (ACP) in Escherichia coli and a variety of plant tissues. In E. coli, ACP is distributed throughout the cytoplasm, confirming the observation of S. Jackowski et al. (1985, J. Bacteriol., 162, 5–8_. In the mesocarp of Avocado (Persea americana) and maturing seeds of oil-seed rape (Brassica napus cv. Jet Neuf), over 95% of the ACP is localised to plastids. The protein is almost exclusively located in the chloroplasts of leaf material from oil-seed rape. Approximately 80% of the gold particles associated with the ACP were further localized to the thylakoid membrane of the chloroplast. Since acetyl-CoA carboxylase has been reported to be localized to the thylakoid membrane (C.G. Kannangara and C.J. Jensen, 1975, Eur. J. Biochem., 54, 25–30), these results are consistent with the view that the two sequential enzymes in fatty-acid synthesis are in close spacial proximity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00392423
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  • 7
    Electronic Resource
    Electronic Resource
    Studies on wheat acetyl CoA carboxylase and the cloning of a partial cDNA (1994)
    Springer
    Plant molecular biology 24 (1994), S. 21-34 
    Details
    ISSN: 1573-5028
    Keywords: acetyl CoA carboxylase ; biotin ; bovine serum albumin ; cDNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Wheat germ acetyl CoA carboxylase (ACCase) was purified by liquid chromatography and electroelution. During purification bovine serum albumin (BSA) was used to coat Amicon membranes used to concentrate partially pure ACCase. Despite further SDS-PAGE/electroelution and microbore HPLC steps BSA remained associated. This presented serious protein sequencing artefacts which may reflect the affinity of BSA for fatty acids bound to ACCase. To avoid these artefacts the enzyme was digested in gel with Endoproteinase LysC protease without the presence of BSA, and the resulting peptides blotted and sequenced. A partial cDNA (1.85 kb) encoding ACCase from a wheat embryo library was cloned, which hybridised to a 7.5 kb RNA species on northern blot of wheat leaf poly(A)+ RNA. The partial cDNA therefore represents about 0.25 of the full-length cDNA. The clone was authenticated by ACCase peptide sequencing and immuno cross-reactivity of the overexpressed clone. The derived amino acid sequence showed homology with both rat and yeast ACCase sequences (62%). Antibodies raised against wheat acetyl CoA carboxylase were specific for a 220 kDa protein from both wheat embryo and leaf. In addition, by using a novel quick assay for ACCase that utilised 125I-streptavidin, we showed the major biotin containing protein to be 220 kDa in both leaf and germ. This is in marked contrast to the previously published molecular mass of 75 kDa allocated to wheat leaf ACCase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00040571
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