Isocitrate dehydrogenase and glyoxylate cycle enzyme activities in Bradyrhizobium japonicum under various growth conditions

1998 ◽  
Vol 169 (5) ◽  
pp. 445-451 ◽  
Author(s):  
L. S. Green ◽  
Dale B. Karr ◽  
David W. Emerich
Keyword(s):  
Isocitrate Dehydrogenase ◽  
Enzyme Activities ◽  
Bradyrhizobium Japonicum ◽  
Glyoxylate Cycle ◽  
Growth Conditions ◽  
Cycle Enzyme

The glyoxylate cycle enzyme activities in the pathogenic isolates of Candida albicans obtained from HIV/AIDS, diabetic and burn patients

Mycoses ◽  
2006 ◽  
Vol 49 (2) ◽  
pp. 85-90 ◽  
Author(s):  
Ali Abdul Lattif ◽  
Rajendra Prasad ◽  
Uma Banerjee ◽  
Nivedita Gupta ◽  
Sameer Mohammad ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Enzyme Activities ◽  
Glyoxylate Cycle ◽  
Burn Patients ◽  
Cycle Enzyme ◽  
The Glyoxylate Cycle ◽  
Hiv Aids

Effect of Leaf Senescence on Glyoxylate Cycle Enzyme Activities

1992 ◽  
Vol 19 (6) ◽  
pp. 723 ◽  
Author(s):  
L Pistelli ◽  
P Perata ◽  
A Alpi
Keyword(s):  
Malate Dehydrogenase ◽  
Enzyme Activities ◽  
Citrate Synthase ◽  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
Malate Synthase ◽  
Cycle Enzyme ◽  
Hydroxypyruvate Reductase ◽  
Foliar Senescence ◽  
The Glyoxylate Cycle

In order to elucidate the metabolism of the peroxisomes during foliar senescence of leaf beet (Beta vulgaris L., var. cicla), peroxisomal activities have been determined at various stages of senescence. Catalase and hydroxypyruvate reductase activities decreased whereas those of the β-oxidation pathway and glyoxylate cycle enzymes increased at the same time. The increased activities of malate synthase, isocitrate lyase, malate dehydrogenase and citrate synthase indicate that the glyoxylate cycle might be activated during the foliar senescence of leaf beet.

Tricarboxylic acid and glyoxylate cycle enzyme activities in Thiobacillus versutus, an isocitrate lyase negative organism

1986 ◽  
Vol 145 (2) ◽  
pp. 148-152 ◽  
Author(s):  
Pieternel A. M. Claassen ◽  
Gerard J. J. Kortstee ◽  
Johannes P. van Dijken ◽  
Wim Harder
Keyword(s):  
Enzyme Activities ◽  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
Tricarboxylic Acid ◽  
Cycle Enzyme ◽  
Thiobacillus Versutus

scholarly journals Changes in Metabolic Enzyme Activities during Thidiazuron-induced Lateral Budbreak of Apple

HortScience ◽  
1991 ◽  
Vol 26 (2) ◽  
pp. 171-173 ◽  
Author(s):  
Shiow Y. Wang ◽  
Hong J. Jiao ◽  
Miklos Faust
Keyword(s):  
Pyruvate Kinase ◽  
Isocitrate Dehydrogenase ◽  
Enzyme Activities ◽  
Tca Cycle ◽  
Tricarboxylic Acid ◽  
Pentose Phosphate ◽  
Rapid Expansion ◽  
Metabolic Enzyme ◽  
Cycle Enzyme ◽  
Glucose 6 Phosphate Dehydrogenase

The activity of glucose-6-phosphate dehydrogenase (G6PDH), 6-phosphate gluconate dehydrogenase (6PGDH), isocitrate dehydrogenase (ICDH), pyruvate kinase (PK), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) were studied in apple (Malus domestics Borkh.) buds during dormancy and thidiazuron-induced budbreak. When buds were dormant, the activity of the glycolytic enzymes GAPDH and PK and the tricarboxylic acid (TCA) cycle enzyme ICDH was low compared to that in nondormant buds. The activity of these enzymes increased during budbreak, peaked when buds were in the green tip stage just before the start of rapid expansion (at 8 days after thidiazuron treatment), and declined thereafter. The activity of pentose-phosphate cycle enzymes G6PDH and 6PGDH was higher in dormant buds than in nondormant buds. 6PGDH was about twice as high as G6PDH. During budbreak and resumption of growth, G6PDH and 6PGDH activity decreased.

Microbodies and glyoxylate-cycle enzyme activities in filamentous fungi

Planta ◽  
1975 ◽  
Vol 124 (2) ◽  
pp. 109-123 ◽  
Author(s):  
D. P. Maxwell ◽  
M. D. Maxwell ◽  
G. H�nssler ◽  
V. N. Armentrout ◽  
G. M. Murray ◽  
...  
Keyword(s):  
Filamentous Fungi ◽  
Enzyme Activities ◽  
Glyoxylate Cycle ◽  
Cycle Enzyme

Co-ordinate regulation of genes involved in storage lipid mobilization in Arabidopsis thaliana

2001 ◽  
Vol 29 (2) ◽  
pp. 283-286 ◽  
Author(s):  
E. L. Rylott ◽  
M. A. Hooks ◽  
I. A. Graham
Keyword(s):  
Arabidopsis Thaliana ◽  
Enzyme Activities ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
Molecular Genetic ◽  
Regulation Of Gene Expression ◽  
Growth Period ◽  
Malate Synthase ◽  
The Glyoxylate Cycle

Molecular genetic approaches in the model plant Arabidopsis thaliana (ColO) are shedding new light on the role and control of the pathways associated with the mobilization of lipid reserves during oilseed germination and post-germinative growth. Numerous independent studies have reported on the expression of individual genes encoding enzymes from the three major pathways: β-oxidation, the glyoxylate cycle and gluconeogenesis. However, a single comprehensive study of representative genes and enzymes from the different pathways in a single plant species has not been done. Here we present results from Arabidopsis that demonstrate the co-ordinate regulation of gene expression and enzyme activities for the acyl-CoA oxidase- and 3-ketoacyl-CoA thiolasemediated steps of β-oxidation, the isocitrate lyase and malate synthase steps of the glyoxylate cycle and the phosphoenolpyruvate carboxykinase step of gluconeogenesis. The mRNA abundance and enzyme activities increase to a peak at stage 2, 48 h after the onset of seed germination, and decline thereafter either to undetectable levels (for malate synthase and isocitrate lyase) or low basal levels (for the genes of β-oxidation and gluconeogenesis). The co-ordinate induction of all these genes at the onset of germination raises the possibility that a global regulatory mechanism operates to induce the expression of genes associated with the mobilization of storage reserves during the heterotrophic growth period.

Isocitrate lyase fromAspergillus nidulans: crystallization and X-ray analysis of a glyoxylate cycle enzyme

1997 ◽  
Vol 53 (4) ◽  
pp. 488-490 ◽  
Author(s):  
S. J. Langridge ◽  
P. J. Baker ◽  
J. R. De Lucas ◽  
S. E. Sedelnikova ◽  
G. Turner ◽  
...  
Keyword(s):  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
X Ray ◽  
Cycle Enzyme
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