Results 151 to 160 of about 1,028 (203)
Stereoselective cycloaddition of 1-glucosyl-1,3-butadienes with tert-butyl 2H-azirine-3-carboxylate, glyoxylates and imines [PDF]
Tetrahedron Letters, 2003 Glucosyl dienes 1 have been reacted with the achiral 2H-azirine 4 and with glyoxylates, forming fused structures of type 5 and disaccharide-like compounds 7 with good to excellent selectivity.
M José Alves, A Gil Fortes
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Metal-catalyzed asymmetric hetero-DielsAlder reactions of unactivated dienes with glyoxylates
Pure and Applied Chemistry, 1998 The development of a catalytic asymmetric hetero-Diels-Alder methodology for the reaction of unactivated dienes with glyoxylates is presented. Several different asymmetric catalysts can be used, but copper-bisoxazolines and aluminium-BINOL give the ...
Mogens Johannsen, Sulan Yao
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The reactions of ureas with glyoxylic acid and methyl glyoxylate
Tetrahedron, 1977Abstract The reactions of urea, methylurea and dimethylureas with glyoxylic acid and its methyl ester to give α-substituted hydantoic acid derivatives ( 4 , 5 , 6 , 7 ) and substituted allantoic acid derivatives ( 8 ) is discussed. The cyclization of the hydantoates and allantoates to 5-substituted hydantoins ( 11 , 12 ) is also described.
Dov Ben-Ishai +2 more
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2009
Some organisms possess enzymes that allow the net conversion of acetyl-CoA to succinate. This is accomplished by the glyoxylate cycle. The overall reaction of this cycle is: 2 acetyl-CoA + NAD + 2 H2O -> succinate + 2 CoA-SH + NADH + H+ As becomes clear from case studies presented, except from prokaryotes, this pathway does not operate as a real ...
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Some organisms possess enzymes that allow the net conversion of acetyl-CoA to succinate. This is accomplished by the glyoxylate cycle. The overall reaction of this cycle is: 2 acetyl-CoA + NAD + 2 H2O -> succinate + 2 CoA-SH + NADH + H+ As becomes clear from case studies presented, except from prokaryotes, this pathway does not operate as a real ...
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Glyoxylate carboligase from E. coli: Specificity of the enzyme for unhydrated glyoxylate
Archives of Biochemistry and Biophysics, 1970Abstract The rate constant of the glyoxylate carboligase-catalyzed condensation of glyoxylate has been measured at high enzyme concentrations. A saturation effect has been observed: the rate constant approaches a limiting value independent of enzyme concentration. Kinetic analysis shows that at these high enzymic rates, the rate-limiting step becomes
R L, Hall, F J, Kézdy
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Thiamine Deficiency and Glyoxylic Acid
Annals of Nutrition and Metabolism, 1981The effect of thiamine deficiency on glyoxylic acid metabolism in mice and rats was investigated to determine whether the vitamin deficiency results in gross effects on glyoxylate levels via an alteration in the activity of alpha-ketoglutarate:glyoxylate carboligase.
C B, Stewart, J, Grammer, R W, Brosemer
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Induction of the glyoxylate cycle in Tetrahymena
Archives of Biochemistry and Biophysics, 1965Abstract The activities of glyoxylate cycle enzymes and the incorporation of acetate-C 14 into metabolic intermediates during the induction of stationary phase in growing cultures of Tetrahymena pyriformis GL were determined. The specific activities of the glyoxylate cycle enzymes, isocitrate lyase and malate synthase, doubled in the stationary ...
M R, LEVY, O H, SCHERBAUM
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The disproportionation of glyoxylate by lactate dehydrogenase
Archives of Biochemistry and Biophysics, 1980Abstract Lactate dehydrogenase (EC 1.1.1.27) catalyzes the NAD-dependent oxidation to (oxalate) and reduction (to glycollate) of glyoxylate. The kinetics of this disproportionation are in accord with the usual reaction pathway of lactate dehydrogenase:substrate inhibition with appropriate pH dependence occurs; a steady state in the ratio of NADH to ...
R. Julian, S. Duncan
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The glyoxylate cycle in Polytomella caeca
Archives of Biochemistry and Biophysics, 1964Abstract 1. 1. The two enzymes unique to the glyoxylate cycle, isocitrate lyase and malate synthase, have been shown to be present in Polytomella caeca . 2. 2. Malate synthase is virtually confined to the particulate fraction. Isocitrate lyase is predominantly cytoplasmic, but is present in small amounts in the particles. 3. 3.
W G, HAIGH, H, BEEVERS
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Glyoxylate as a Substrate for Lactate Dehydrogenase
Nature, 1967IF 2-oxobutyrate is substituted for pyruvate as substrate for lactate dehydrogenase (LD), it is found to be more readily reduced by the electrophoretically faster moving LD isoenzymes than by the slower moving LD isoenzymes1,2. Because glyoxylate may also serve as a substrate for LD (ref. 3), we investigated the effect of LD isoenzyme fractions on this
M R, Banner, S B, Rosalki
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