Results 171 to 180 of about 16,670 (212)
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Glyoxylate Cycle

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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Particulate enzymes of the glyoxylate cycle in Neurospora crassa

Biochemical and Biophysical Research Communications, 1969
Abstract A particle carrying at least some of the enzymes of the glyoxylate cycle was found in Neurospora crassa . This particle has a density different from that of the mitochondrion. The proportion of the isocitrate lyase bound to this particle varies with the composition of the carbon source.
Francine Vanderhaeghe   +2 more
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Re-examining the role of the glyoxylate cycle in oilseeds

Trends in Plant Science, 2001
Oil is the primary seed storage reserve in many higher plants. After germination, this reserve is mobilized in order to support growth during early seedling development. The glyoxylate cycle is instrumental in this metabolic process. It allows acetyl-CoA derived from the breakdown of storage lipids to be used for the synthesis of carbohydrate. Recently,
Ian A. Graham, Peter J. Eastmond
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Evidences of glyoxylate cycle in peroxisomes of senescent cotyledons

Plant Science, 1995
Abstract The metabolic pathway of the glyoxylate cycle has been investigated in peroxisomes isolated from senescent pumpkin ( Cucurbita sp.) cotyledons. β-oxidation activity, as well as activities of glyoxylate cycle enzymes isocitrate lyase (EC 4.1.3.1), malate synthase (EC 4.1.3.2), malate dehydrogenase (EC 1.1.1.37) and citrate synthase (EC 4.1.3.
PISTELLI, LAURA   +2 more
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Tricarboxylic acid and glyoxylate cycles in the "Leishmaniae"

Acta tropica, 1977
Cell-free extacts of four species of Leishmania (L. brasiliensis, L. donovani, L. mexicana and L. tropica) have been shown to contain all enzymes of the tricarboxylic acid cycle. However, the activity of citrate synthase is so low that it is doubtful whether this pathway is of significance in the metabolism of carbohydrate substrates.
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The Glyoxylate Cycle in Germinating Ginkgo biloba Seeds

Canadian Journal of Biochemistry, 1973
The high level of lipids in Ginkgo biloba seeds suggested that the glyoxylate cycle is operative during germination. The correlation between the lipid content of germinating seeds and the key-enzyme levels of the cycle were studied. The fatty acid composition and content of the triglyceride fraction during germination were also investigated.
VANNI, PAOLO   +3 more
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Inhibition of the Krebs cycle by glyoxylic acid

Phytochemistry, 1969
Abstract Evidence is presented that glyoxylic acid inhibits the Krebs cycle activity of pea mitochondria. The extent and nature of the inhibition is compared with the inhibition produced by 4-hydroxy-2-oxoglutarate. It is argued that inhibition by glyoxylate is direct and does not require prior condensation with oxaloacetate or pyruvate.
David D. Davies, Gilles Ribereau-Gayon
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Synthesis and Function of Glyoxylate Cycle Enzymes

2002
The glyoxylate cycle in plants has been the subject of much research for several decades, and many hundreds of primary research papers have been published. There have been numerous reviews covering different aspects of the synthesis and function of glyoxylate cycle enzymes (Beevers, 1979; Trelease, 1984; Escher and Widmer 1997; Eastmond and Graham ...
Johanna E. Cornah, Steven M. Smith
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The tricarboxylic acid cycle and the glyoxylate bypass

2004
The oxidative decarboxylation of pyruvate to form acetyl CoA, which occurs in the mitichondrial matrix in eukaryotes, is the link between glycolysis and the tricarboxylic (or citric) acid cycle.
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Localization of Glyoxylate Cycle Enzymes in Glyoxysomes in Euglena*

The Journal of Protozoology, 1972
SYNOPSIS. We demonstrated previously microbodies in Euglena gracilis grown in the dark on 2‐carbon substrates. We have now established in Euglena the particulate nature of enzymes known in other organisms to be localized in microbodies (glyoxysomes and leaf peroxisomes).
Albin Grill   +3 more
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