Purification of the Glyoxylate Cycle Enzyme Malate Synthase from Maize (Zea mays L) and Characterization of a Proteolytic Fragment

1993 ◽  
Vol 4 (6) ◽  
pp. 519-528 ◽  
Author(s):  
A.S. Khan ◽  
E. Vandriessche ◽  
L. Kanarek ◽  
S. Beeckmans
Keyword(s):  
Zea Mays ◽  
Zea Mays L ◽  
Glyoxylate Cycle ◽  
Malate Synthase ◽  
Proteolytic Fragment ◽  
Cycle Enzyme ◽  
The Glyoxylate Cycle

Characterization of a Bifunctional Glyoxylate Cycle Enzyme, Malate Synthase/Isocitrate Lyase, of Euglena gracilis

2011 ◽  
Vol 58 (2) ◽  
pp. 128-133 ◽  
Author(s):  
MASAMI NAKAZAWA ◽  
MASAAKI NISHIMURA ◽  
KENGO INOUE ◽  
MITSUHIRO UEDA ◽  
HIROSHI INUI ◽  
...  
Keyword(s):  
Euglena Gracilis ◽  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
Malate Synthase ◽  
Cycle Enzyme

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.

TheglcBlocus ofRhizobium leguminosarumVF39 encodes an arabinose-inducible malate synthase

2002 ◽  
Vol 48 (10) ◽  
pp. 922-932 ◽  
Author(s):  
Alejandro García-de los Santos ◽  
Alejandro Morales ◽  
Laura Baldomá ◽  
Scott R.D Clark ◽  
Susana Brom ◽  
...  
Keyword(s):  
Sinorhizobium Meliloti ◽  
Rhizobium Leguminosarum ◽  
Plant Cell Wall ◽  
Glyoxylate Cycle ◽  
Malate Synthase ◽  
Mesorhizobium Loti ◽  
Malate Synthase G ◽  
Similar Genome Organization ◽  
The Glyoxylate Cycle

In the course of a study conducted to isolate genes upregulated by plant cell wall sugars, we identified an arabinose-inducible locus from a transcriptional fusion library of Rhizobium leguminosarum VF39, carrying random insertions of the lacZ transposon Tn5B22. Sequence analysis of the locus disrupted by the transposon revealed a high similarity to uncharacterized malate synthase G genes from Sinorhizobium meliloti, Agrobacterium tumefaciens, and Mesorhizobium loti. This enzyme catalyzes the condensation of glyoxylate and acetyl-CoA to yield malate and CoA and is thought to be a component of the glyoxylate cycle, which allows microorganisms to grow on two carbon compounds. Enzyme assays showed that a functional malate synthase is encoded in the glcB gene of R. leguminosarum and that its expression is induced by arabinose, glycolate, and glyoxylate. An Escherichia coli aceB glcB mutant, complemented with the R. leguminosarum PCR-amplified gene, recovered malate synthase activity. A very similar genome organization of the loci containing malate synthase and flanking genes was observed in R. leguminosarum, S. meliloti, and A. tumefaciens. Pea plants inoculated with the glcB mutant or the wild-type strain showed no significant differences in nitrogen fixation. This is the first report regarding the characterization of a mutant in one of the glyoxylate cycle enzymes in the rhizobia.Key words: Rhizobium, malate synthase, glyoxylate cycle, arabinose metabolism.

scholarly journals Lipid Utilization, Gluconeogenesis, and Seedling Growth inArabidopsisMutants Lacking the Glyoxylate Cycle Enzyme Malate Synthase

2004 ◽  
Vol 279 (41) ◽  
pp. 42916-42923 ◽  
Author(s):  
Johanna E. Cornah ◽  
Véronique Germain ◽  
Jane L. Ward ◽  
Michael H. Beale ◽  
Steven M. Smith
Keyword(s):  
Seedling Growth ◽  
Glyoxylate Cycle ◽  
Malate Synthase ◽  
Cycle Enzyme ◽  
Lipid Utilization ◽  
The Glyoxylate Cycle

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.

scholarly journals Characterization of phenylpropanoid pathway genes within European maize (Zea mays L.) inbreds

2008 ◽  
Vol 8 (1) ◽  
pp. 2 ◽  
Author(s):  
Jeppe Andersen ◽  
Imad Zein ◽  
Gerhard Wenzel ◽  
Birte Darnhofer ◽  
Joachim Eder ◽  
...  
Keyword(s):  
Zea Mays ◽  
Zea Mays L ◽  
Phenylpropanoid Pathway ◽  
European Maize

scholarly journals Characterization of corn (Zea mays L.) bran as a new food ingredient for snack bars

LWT ◽  
2019 ◽  
Vol 101 ◽  
pp. 812-818 ◽  
Author(s):  
Milena Figueiredo de Sousa ◽  
Rafaiane Macedo Guimarães ◽  
Marcos de Oliveira Araújo ◽  
Keyla Rezende Barcelos ◽  
Nárgella Silva Carneiro ◽  
...  
Keyword(s):  
Zea Mays ◽  
Zea Mays L ◽  
Food Ingredient
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