Results 121 to 130 of about 2,753 (185)
Properties and distribution of mammalian l-cysteine sulfinate carboxy-lyases
Biochimica Et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964 Abstract 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.
J G, JACOBSEN, L L, THOMAS, L H, SMITH
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Biologically generated carbon dioxide: nature's versatile chemical strategies for carboxy lyases
Natural Product Reports, 2020 Metabolic 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, 1994 L-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.
Tomader A. El-Rahmany
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O-pyrocatechuic acid carboxy-lyase from Aspergillus niger
Archives of Biochemistry and Biophysics, 1967 Abstract 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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Biochimica et Biophysica Acta (BBA) - Biomembranes, 1976 A sensitive and quantitative assay for 3-octaprenyl-4-hydroxybenzoate carboxy-lyase has been developed. This enzyme, which catalyses the third reaction in ubiquinone biosynthesis in Escherichia coli, was partially purified and some of its properties determined.
R A, Leppik, I G, Young, F, Gibson
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Biochemie und Physiologie der Pflanzen, 1977 Summary Orotidine-5′-phosphate: pyrophosphate-phosphoribosyltransferase and orotidine-5′-phosphate: carboxy-lyase were characterized in a crude extract from Euglena gracilis. Z The coupled enzyme reaction was measured by 14 CO 2 release from [7- 14 C]-orotic acid. Characteristics of the enzyme system are an apparent K m value for orotate of 17 μ
W. Rattke, G.-J. Krauss
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Porphyrin biosynthesis. X. Porphyrinogen carboxy-lyase from avian erythrocytes futher properties
Biochimica et Biophysica Acta (BBA) - Enzymology, 1973 Abstract 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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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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Glyoxylate carboxy-lyase activity in the unicellular green alga gloemonas SP.
Biochimica et Biophysica Acta (BBA) - Enzymology, 1971 Abstract 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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L-Arginine carboxy-lyase of higher plants and its relation to potassium nutrition
Phytochemistry, 1963 Abstract On a fresh weight basis the mean agmatine content was found to be eight times as high, and the mean L -arginine carboxy-lyase (arginine decarboxylase) activity twice as high in leaves of potassium-deficient barley plants as in leaves of normal barley plants. A range of other plant species was also shown to accumulate agmatine and putrescine
T.A. Smith
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