Results 211 to 220 of about 114,163 (257)
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The Journal of Parasitology, 1981
The rate of 14CO2 evolution from 1-[14C]pyruvate by intact Ascaris mitochondria was very slow, but increased with increasing concentrations of pyruvate. At all concentrations of pyruvate, in an aerobic environment, pyruvate decarboxylation was stimulated greatly by the addition of fumarate, malate, or succinate.
R. Komuniecki, P. Komuniecki, H. J. Saz
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The rate of 14CO2 evolution from 1-[14C]pyruvate by intact Ascaris mitochondria was very slow, but increased with increasing concentrations of pyruvate. At all concentrations of pyruvate, in an aerobic environment, pyruvate decarboxylation was stimulated greatly by the addition of fumarate, malate, or succinate.
R. Komuniecki, P. Komuniecki, H. J. Saz
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[Pyruvate decarboxylation in homofermenter lactobacilli].
Revista latinoamericana de microbiologia, 1975 de Cádenas Lb +2 more
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Decarboxylation of glyoxylate by a pyruvate oxidase in Lactobacillus plantarum
International Journal of Biochemistry, 1975 Abstract 1. 1. An enzyme that oxidatively decarboxylates glyoxylate was purified 237-fold from Lactobacillus plantarum , and resolved by electrofocusing from other enzymes known to act on glyoxylate. 2. 2. The enzyme is a flavoprotein stimulated by thiamine pyrophosphate and FAD. NAD or NADP did not replace FAD. 3. 3. The reaction is not
Nabila Turujman, I.F. Durr
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A thiamin-utilizing ribozyme decarboxylates a pyruvate-like substrate
Nature Chemistry, 2013Vitamins are hypothesized to be relics of an RNA world, and were probably participants in RNA-mediated primordial metabolism. If catalytic RNAs, or ribozymes, could harness vitamin cofactors to aid their function in a manner similar to protein enzymes, it would enable them to catalyse a much larger set of chemical reactions.
Paul, Cernak, Dipankar, Sen
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Decarboxylation and carboxylation of pyruvate in the living mice
Biochimie, 1979Mice received intravenously [1- or 2-14C]acetate, [1-, 2- or 3-14C] or [2-14C]pyruvate and were killed 1, 3, 5 or 15 min later. The radioactivity of CO2 or HCO3- of liver or carcass as well as the radioactivity of blood glucose were measured. The ratio of the radioactivity found in these compounds after [3-14C] or [2-14C-A1pyruvate injection suggests ...
P, Favarger, S, Rous, S, Bas
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Attempts to inhibit ruminal methanogenesis by blocking pyruvate oxidative decarboxylation
Canadian Journal of Microbiology, 2003The inhibition of pyruvate oxidative decarboxylation as a means of decreasing ruminal methanogenesis in vitro was studied. In the first experiment, the addition of adenosine and adenine (with and without ribose) to ruminal batch cultures did not decrease methanogenesis. In the second experiment, the addition of oxythiamin decreased methanogenesis by 23%
E M, Ungerfeld, S R, Rust, R, Burnett
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Pyruvate decarboxylating activity in extracts from pigeon liver acetone powder
Biochemical Medicine, 1983Extracts of pigeon liver acetone powder showed, by a radiochemical method, considerable pyruvate decarboxylating activity. The 10-30% saturated ammonium sulfate fraction of these extracts required the addition of CoA, NAD+, and TPP for maximum pyruvate decarboxylating activity and presumably contained the pyruvate dehydrogenase complex (PDHC).
G, Constantopoulos, J A, Barranger
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Archiv f�r Mikrobiologie, 1969 1. It has been confirmed that under anaerobic conditions at pH 2 pyruvic acid is vigorously decarboxylated by intact baker's yeast, but hardly at all at pH 5.5. Furthermore, the decarboxylation occurs more slowly with semiaerobically cultured than with aerobically cultured baker's yeast. 2.
Heikki Suomalainen +2 more
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Decarboxylation of pyruvic acid in aqueous solution by thermal proteinoids
Archives of Biochemistry and Biophysics, 1968Abstract Thermal proteinoids accelerate the conversion of pyruvic acid to carbon dioxide and acetic acid. The reaction follows Michaelis-Menten kinetics. Co-poly(glutamic acid-threonine) and co-poly (glutamic acid-leucine) were found to be the most active of simple co-polymers and even more active than proteinoid.
H G, Hardebeck, G, Krampitz, L, Wulf
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Why Saccharomyces cerevisiae can oxidize but not decarboxylate external pyruvate
Biochimica et Biophysica Acta (BBA) - General Subjects, 1996Protoplasts of the yeast Saccharomyces cerevisiae oxidized externally added pyruvate by pyruvate oxidase system but were not able to decarboxylate it anaerobically by pyruvate decarboxylase at pH 6.4 in isotonic solutions. The decarboxylation set in hypotonic solutions in which the integrity of the plasma membrane was being impaired.
L, Kovác, C A, Stella, E H, Ramos
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