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

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.

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The Sinorhizobium meliloti glyoxylate cycle enzyme isocitrate lyase (AceA) is required for the utilization of poly-β-hydroxybutyrate during carbon starvation

Annals of Microbiology ◽

10.1007/s13213-015-1131-0 ◽

2015 ◽

Vol 66 (2) ◽

pp. 921-924

Author(s):

José Augusto Ramírez-Trujillo ◽

Michael F. Dunn ◽

Ramón Suárez-Rodríguez ◽

Ismael Hernández-Lucas

Keyword(s):

Sinorhizobium Meliloti ◽

Isocitrate Lyase ◽

Glyoxylate Cycle ◽

Carbon Starvation ◽

Cycle Enzyme

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

Archives of Microbiology ◽

10.1007/bf00446772 ◽

1986 ◽

Vol 145 (2) ◽

pp. 148-152 ◽

Cited By ~ 5

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

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Molecular characterization of a bifunctional glyoxylate cycle enzyme, malate synthase/isocitrate lyase, in Euglena gracilis

Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology ◽

10.1016/j.cbpc.2005.05.006 ◽

2005 ◽

Vol 141 (4) ◽

pp. 445-452 ◽

Cited By ~ 12

Author(s):

Masami Nakazawa ◽

Tomomi Minami ◽

Koji Teramura ◽

Shohei Kumamoto ◽

Sayaka Hanato ◽

...

Keyword(s):

Molecular Characterization ◽

Euglena Gracilis ◽

Isocitrate Lyase ◽

Glyoxylate Cycle ◽

Malate Synthase ◽

Cycle Enzyme

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

Biochemical Society Transactions ◽

10.1042/bst0290283 ◽

2001 ◽

Vol 29 (2) ◽

pp. 283-286 ◽

Cited By ~ 54

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.

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Molecular analysis of the Penicillium marneffei glyceraldehyde-3-phosphate dehydrogenase-encoding gene (gpdA) and differential expression of gpdA and the isocitrate lyase-encoding gene (acuD) upon internalization by murine macrophages

Journal of Medical Microbiology ◽

10.1099/jmm.0.2008/002832-0 ◽

2008 ◽

Vol 57 (11) ◽

pp. 1322-1328 ◽

Cited By ~ 15

Author(s):

Sophit Thirach ◽

Chester R. Cooper ◽

Nongnuch Vanittanakom

Keyword(s):

Differential Expression ◽

Isocitrate Lyase ◽

Glyoxylate Cycle ◽

Evolutionary Relationship ◽

Amino Acid Sequences ◽

Penicillium Marneffei ◽

Macrophage Infection ◽

Dimorphic Fungus ◽

Isolation And Characterization ◽

Encoding Gene

Penicillium marneffei is an intracellular dimorphic fungus that can cause a fatal disseminated disease in human immunodeficiency virus-infected patients. The factors that affect the pathogenicity of this fungus remain unclear. Here, we report the isolation and characterization of the gpdA cDNA and genomic clones encoding glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in P. marneffei. Phylogenetic analysis of GAPDH amino acid sequences demonstrated the evolutionary relationship of P. marneffei to other fungi, including the intracellular pathogen Ajellomyces capsulatus. To assess the central importance of phagocytic cells in defence against P. marneffei infection, we used Northern blotting to investigate the response of the isocitrate lyase-encoding gene (acuD) and gpdA to nutrient deprivation inside macrophages. The results revealed that after macrophage internalization, the gene involved in the glyoxylate cycle, acuD, showed higher expression levels as early as 2 h from the start of co-incubation, and the differential expression could be observed again at 8 h after infection. In contrast, the expression of gpdA was downregulated in the yeast phase, as well as during macrophage infection after 2, 4 and 8 h of infection. The induction of P. marneffei acuD was shown to be coordinated with the downregulation of the glycolytic gpdA gene, implying that the cytoplasmic environment of macrophages is deficient in glucose and the glyoxylate pathway could be used by this pathogen to allow subsistence on two-carbon compounds within the host cell following its intracellular persistence.

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Whole-Genome Transcriptional Profiling of Bradyrhizobium japonicum during Chemoautotrophic Growth

Journal of Bacteriology ◽

10.1128/jb.00543-08 ◽

2008 ◽

Vol 190 (20) ◽

pp. 6697-6705 ◽

Cited By ~ 24

Author(s):

William L. Franck ◽

Woo-Suk Chang ◽

Jing Qiu ◽

Masayuki Sugawara ◽

Michael J. Sadowsky ◽

...

Keyword(s):

Bradyrhizobium Japonicum ◽

Carbon Fixation ◽

Cultured Cells ◽

Isocitrate Lyase ◽

Nitrogenase Activity ◽

Glyoxylate Cycle ◽

Transcriptional Profiling ◽

Pentose Phosphate ◽

Hydrogen Gas ◽

Essential Components

ABSTRACT Bradyrhizobium japonicum is a facultative chemoautotroph capable of utilizing hydrogen gas as an electron donor in a respiratory chain terminated by oxygen to provide energy for cellular processes and carbon dioxide assimilation via a reductive pentose phosphate pathway. A transcriptomic analysis of B. japonicum cultured chemoautotrophically identified 1,485 transcripts, representing 17.5% of the genome, as differentially expressed when compared to heterotrophic cultures. Genetic determinants required for hydrogen utilization and carbon fixation, including the uptake hydrogenase system and components of the Calvin-Benson-Bassham cycle, were strongly induced in chemoautotrophically cultured cells. A putative isocitrate lyase (aceA; blr2455) was among the most strongly upregulated genes, suggesting a role for the glyoxylate cycle during chemoautotrophic growth. Addition of arabinose to chemoautotrophic cultures of B. japonicum did not significantly alter transcript profiles. Furthermore, a subset of nitrogen fixation genes was moderately induced during chemoautotrophic growth. In order to specifically address the role of isocitrate lyase and nitrogenase in chemoautotrophic growth, we cultured aceA, nifD, and nifH mutants under chemoautotrophic conditions. Growth of each mutant was similar to that of the wild type, indicating that the glyoxylate bypass and nitrogenase activity are not essential components of chemoautotrophy in B. japonicum.

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Acetate metabolism in Escherichia coli

Canadian Journal of Microbiology ◽

10.1139/m78-027 ◽

1978 ◽

Vol 24 (2) ◽

pp. 149-153 ◽

Cited By ~ 5

Author(s):

T. M. Lakshmi ◽

Robert B. Helling

Keyword(s):

Isocitrate Dehydrogenase ◽

Citrate Synthase ◽

Isocitrate Lyase ◽

Glyoxylate Cycle ◽

Acetate Metabolism ◽

Wild Type ◽

Intermediary Metabolites ◽

Lyase Activity ◽

Acetate Medium ◽

The Glyoxylate Cycle

Levels of several intermediary metabolites were measured in cells grown in acetate medium in order to test the hypothesis that the glyoxylate cycle is repressed by phosphoenolpyruvate (PEP). Wild-type cells had less PEP than either isocitrate dehydrogenase – deficient cells (which had greater isocitrate lyase activity than the wild type) or isocitrate dehydrogenase – deficient, citrate synthase – deficient cells (which are poorly inducible). Thus induction of the glyoxylate cycle is more complicated than a simple function of PEP concentration. No correlation between enzyme activity and the level of oxaloacetate, pyruvate, or citrate was found either. Citrate was synthesized in citrate synthase – deficient mutants, possibly via citrate lyase.

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