Results 81 to 90 of about 2,651 (134)
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Properties and distribution of mammalian l-cysteine sulfinate carboxy-lyases
Biochimica Et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964Abstract 1. 1. [1-14C]Cysteine sulfinic acid (CySO2H) and [1-14C]cysteic acid (CySO3H) were synthesized and some characteristics of the decarboxylation of these amino acids studied in partially purified rat-liver and brain preparations. 2. 2. The apparent Km's for CySO2H and CySO3H were found to be about 10 times lower in liver than in brain.
Lloyd H Smith, L L Thomas
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Biologically generated carbon dioxide: nature's versatile chemical strategies for carboxy lyases
Natural Product Reports, 2020Metabolic production of CO2is natural product chemistry on a mammoth scale.
Christopher T Walsh
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Comparison of L-aspartate 4-carboxy-lyases ofCunninghamella elegansandPenicillium citrinum
Microbiological Research, 1994L-Aspartate 4-carboxy-lyase of Cunninghamella elegans and Penicillium citrinum has a pH optimum of 5.5. Maximal activity of both enzymes is obtained at 40 degrees C, and both are thermolabile. The Km of the C. elegans enzyme for L-aspartate is 25 mM, while that of the P. citrinum enzyme is 27 mM. The two enzymes are specific for L-aspartate.
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O-pyrocatechuic acid carboxy-lyase from Aspergillus niger
Archives of Biochemistry and Biophysics, 1967Abstract O -Pyrocatechuic acid (2,3-dihydroxybenzoic acid) carboxylyase (E.C. 4.1.1.), enzyme involved in the biosynthesis of catechol by Aspergillus niger , has been extracted from the acetone powders of mycelial mats grown in the presence of l -tryptophan and purified 815-fold by precipitation of nucleic acids, fractionation with ammonium ...
P V, Rao, K, Moore, G H, Towers
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Studies on Porphyrinogen Carboxy-Lyase from Chick Embryo Liver
Enzyme, 2017The purpose of the present work was to find the optimal conditions for the assay of chick embryo liver porphyrinogen carboxy-lyase. The enzyme activity was studied as a function of protein and substrate concentrations, time, pH value and incubation temperature.
M C, Taira, L C, San Martín de Viale
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Stereochemistry of porphyrinogen carboxy-lyase reaction in haem biosynthesis
Journal of the Chemical Society, Chemical Communications, 1975Stereospecifically deuteriated and tritiated succinate was incorporated into the acetate residues of uroporphyrinogen III which on decarboxylation generated asymmetric methyl groups in coproporphyrinogen III and then in haem; degradation of the latter yielded chiral acetate deriving from the C and D rings of haem and configurational analysis of this ...
Graham F. Barnard, Muhammad Akhtar
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Glyoxylate carboxy-lyase activity in the unicellular green alga gloemonas SP.
Biochimica et Biophysica Acta (BBA) - Enzymology, 1971Abstract Glyoxylate carboxy-lyase (also known as glyoxylate carboligase, systematic name: glyoxylate carboxy-lase (dimerizing and reducing)) activity has been demonstrated in cell-free extracts prepared from the photoautotrophically grown unicellular green alga Gloeomonas.
S S, Badour, E R, Waygood
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International Journal of Biochemistry, 1980
Abstract 1. 1. It has been reported that hexachlorobenzene (HCB) in vivo produces hepatic porphyrinogen carboxy-lyase (PCL) decrease and pentachlorophenol (PCP) is one of its metabolites. In order to investigate if such decrease is due to an enzyme inhibitor present in the porphyric livers, the effects of the following additions on the normal rat
M C, Rios de Molina +2 more
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Abstract 1. 1. It has been reported that hexachlorobenzene (HCB) in vivo produces hepatic porphyrinogen carboxy-lyase (PCL) decrease and pentachlorophenol (PCP) is one of its metabolites. In order to investigate if such decrease is due to an enzyme inhibitor present in the porphyric livers, the effects of the following additions on the normal rat
M C, Rios de Molina +2 more
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Porphyrin biosynthesis. X. Porphyrinogen carboxy-lyase from avian erythrocytes futher properties
Biochimica et Biophysica Acta (BBA) - Enzymology, 1973Abstract Several properties of porphyrinogen carboxy-lyase from normal chicken erythrocytes were studied. 1. 1. The utilization of the substrate uroporphyrinogen (8-COOH), and the formation of intermediate products (porphyrinogens of 7-, 6- and 5-COOH) and the final product coproporphyrinogen (4-COOH) were investigated as function of time and ...
R C, Garcia +3 more
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Clinica Chimica Acta, 1980
Red cell porphyrinogen carboxy-lyase activity was measured using uroporphyrinogen III as substrate in 18 normal persons, 7 male patients with porphyria cutanea tarda, 3 female patients with erythropoietic protoporphyria and 2 female patients with variegate porphyria.
M C, Ríos de Molina +3 more
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Red cell porphyrinogen carboxy-lyase activity was measured using uroporphyrinogen III as substrate in 18 normal persons, 7 male patients with porphyria cutanea tarda, 3 female patients with erythropoietic protoporphyria and 2 female patients with variegate porphyria.
M C, Ríos de Molina +3 more
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