Results 151 to 160 of about 156,688 (202)
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[Characterization and properties of two dehydroquinate hydro-lyases in higher plants].
Planta, 2014Two dehydroquinate hydro-lyases (E.C. 4.2.1.10) have been routinely separated from different organs of Zea mays L. by chromatography on Cellex-D Bio-Rad or hydroxypatite using linear salt gradients. Dehydroquinate hydro-lyase 1 is associated with shikimate: NADP(+) oxidoreductase (E.C. 1.1.1.25).
A M, Boudet, R, Lécussan, A, Boudet
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European Journal of Biochemistry, 1987
d‐Altronate hydratase and d‐mannonate hydratase belong to a class of Fe2+‐requiring enzymes, but the function of iron in these enzymes is largely unknown. Methods are described for the convenient preparation of both these hydratases from Escherichia coli and studies related to metal activation are presented.
Jean-Luc Dreyer
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d‐Altronate hydratase and d‐mannonate hydratase belong to a class of Fe2+‐requiring enzymes, but the function of iron in these enzymes is largely unknown. Methods are described for the convenient preparation of both these hydratases from Escherichia coli and studies related to metal activation are presented.
Jean-Luc Dreyer
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Indoleacetaldoxime hydro-lyase
Archives of Biochemistry and Biophysics, 1968The purification and some properties of the enzyme indoleacetaldoxime hydrolyase (EC 4.2.1.29) from the fungus Gibberella fujikuroi, which dehydrates indoleacetaldoxime (IAOX) to indoleacetonitrile (IAN), are described. The enzyme activity in the fungus is present only under certain culture conditions.
P.S. Shukla, S. Mahadevan
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BIOSYNTHESIS OF PORPHYRINS IN WHEAT LEAVES: II. 5-AMINOLAEVULINATE HYDRO-LYASE
Canadian Journal of Biochemistry, 19675-Aminolaevulinate hydro-lyase (EC 4.2.1.24), which catalyzes the formation of porphobilinogen from 5-aminolaevulinate (5-ALA), was isolated from wheat leaves and partially purified. The enzyme was specific for 5-ALA, sulfhydryl-dependent, and required divalent cations for maximum activation.
D L, Nandi, E R, Waygood
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3-Dehydroshikimate hydro-lyase ofPhaseolus mungo seedlings
The Botanical Magazine Tokyo, 19723-Dehydroshikimate hydro-lyase was extracted and partially purified by ammonium sulfate fractionation from the hypocotyls of etiolatedPhaseolus mungo seedings. The enzyme was most active at pH 7.0 and the Km for DHS was 1.4 mM. Enzyme activity was inhibited byp-chloromercuribenzoate and arsenite, the inhibition being reversed by reduced glutathione ...
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Morphological changes at Nhat Le estuary under hydro-meteorological influence
Journal of Hydro-meteorology: Nhat Le estuary is located on the Central coast of Viet Nam, where it always has strong morphological changes under the influence of seasonal changing dynamic factors.
Dinh Cuong Vu +2 more
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Purification and Properties of Crystalline 2-Phospho-d-Glycerate Hydro-Lyase from Human Muscle
European Journal of Biochemistry, 19681 The purification and crystallization of 2-phospho-d-glycerate hydro-lyase from human skeletal muscle is described. 2 Preparations of the crystalline enzyme were found to be homogenous as examined in free boundary and gel electrophoresis. Chromatography on Sephadex G 75 and TEAE-cellulose revealed only one component.
T, Baranowski, E, Wolna, A, Morawiecki
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Pork liver has been shown to contain a soluble enzyme, L-fuconate hydro-lyase (L-fuconate dehydratase), capable of dehydrating L-fuconate to 2-keto-3-deoxy-L-fuconate. The enzyme has been partially purified. The Km for L-fuconate is 1.0 mM; D-arabonate is also an excellent substrate (Km 1.3 mM) but the enzyme is inactive with D-fuconate, L-arabonate ...
R, Yuen, H, Schachter
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Isolation and biochemical characterization of maleic‐acid hydratase, an iron‐requiring hydro‐lyase
European Journal of Biochemistry, 1985A procedure for the isolation of maleic acid hydratase (D‐malete hydro‐lyase, EC 4.2.1.31) of about 95% purity from rabbit kidneys is described. The enzyme consists of a single polypeptide chain of 582 amino‐acid residues with an approximate molecular mass of 68 kDa.
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[Individuality of mannonate and altronate hydro-lyases in Escherichia coli K 12].
Biochimie, 1975In Escherichia coli, mannonic and altronic hydrolyases act, respectively, on mannonate, the intermediate aldonate of the glucuronate branch, and on altronate the intermediate aldonate of the galacturonate branch of the hexuronate pathway, yielding 2-keto-3-deoxy-gluconate.
J M, Robert-Baudouy +2 more
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