Results 131 to 140 of about 87,290 (186)
Some of the next articles are maybe not open access.
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
openaire +4 more sources
Immobilisation of hydroxynitrile lyases
Chemical Society Reviews, 2013 Hydroxynitrile lyases are a versatile group of enzymes that are applied both in the laboratory and on an industrial scale. What makes them particularly interesting is that to date five structurally unrelated categories of hydroxynitrile lyases have been ...
Ulf Hanefeld
exaly +2 more sources
[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
openaire +4 more sources
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
openaire +2 more sources
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 ...
openaire +1 more source
Identification of two [4Fe–4S]-cluster-containing hydro-lyases from Pyrococcus furiosus
Microbiology, 2009The hyperthermophilic archaeonPyrococcus furiosusis a strict anaerobe. It is therefore not expected to use the oxidative tricarboxylic acid (TCA) cycle for energy transduction. Nonetheless, its genome encodes more putative TCA cycle enzymes than the closely relatedPyrococcus horikoshiiandPyrococcus abyssi, including an aconitase (PF0201).
Barbara M A, van Vugt-Lussenburg +3 more
openaire +2 more sources
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
openaire +2 more sources
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.
openaire +2 more sources
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
openaire +2 more sources
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.
openaire +2 more sources
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.
openaire +2 more sources