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

2005 ◽  
Vol 141 (4) ◽  
pp. 445-452 ◽  
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

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.

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

Purification and Characterization of Isocitrate Lyase from Ethanol-grown Euglena gracilis

1994 ◽  
Vol 41 (6) ◽  
pp. 536-539 ◽  
Author(s):  
KOUKI ONO ◽  
MASAHIRO OKIHASHI ◽  
HIROSHI INUI ◽  
KAZUTAKA MIYATAKE ◽  
SHOZABURO KITAOKA ◽  
...  
Keyword(s):  
Euglena Gracilis ◽  
Isocitrate Lyase ◽  
Purification And Characterization

Molecular characterization of a calmodulin involved in the signal transduction chain of gravitaxis in Euglena gracilis

Planta ◽  
2010 ◽  
Vol 231 (5) ◽  
pp. 1229-1236 ◽  
Author(s):  
Viktor Daiker ◽  
Michael Lebert ◽  
Peter Richter ◽  
Donat-Peter Häder
Keyword(s):  
Signal Transduction ◽  
Molecular Characterization ◽  
Euglena Gracilis

scholarly journals Identification of RamA, a Novel LuxR-Type Transcriptional Regulator of Genes Involved in Acetate Metabolism of Corynebacterium glutamicum

2006 ◽  
Vol 188 (7) ◽  
pp. 2554-2567 ◽  
Author(s):  
Annette Cramer ◽  
Robert Gerstmeir ◽  
Steffen Schaffer ◽  
Michael Bott ◽  
Bernhard J. Eikmanns
Keyword(s):  
Corynebacterium Glutamicum ◽  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
Transcriptional Regulator ◽  
Malate Synthase ◽  
Acetate Kinase ◽  
Acetate Metabolism ◽  
Promoter Regions ◽  
Cell Extracts ◽  
Peptide Mass

ABSTRACT In Corynebacterium glutamicum, the acetate-activating enzymes phosphotransacetylase and acetate kinase and the glyoxylate cycle enzymes isocitrate lyase and malate synthase are coordinately up-regulated in the presence of acetate in the growth medium. This regulation is due to transcriptional control of the respective pta-ack operon and the aceA and aceB genes, brought about at least partly by the action of the negative transcriptional regulator RamB. Using cell extracts of C. glutamicum and employing DNA affinity chromatography, mass spectrometry, and peptide mass fingerprinting, we identified a LuxR-type transcriptional regulator, designated RamA, which binds to the pta-ack and aceA/aceB promoter regions. Inactivation of the ramA gene in the genome of C. glutamicum resulted in mutant RG2. This mutant was unable to grow on acetate as the sole carbon and energy source and, in comparison to the wild type of C. glutamicum, showed very low specific activities of phosphotransacetylase, acetate kinase, isocitrate lyase, and malate synthase, irrespective of the presence of acetate in the medium. Comparative transcriptional cat fusion experiments revealed that this deregulation takes place at the level of transcription. By electrophoretic mobility shift analysis, purified His-tagged RamA protein was shown to bind specifically to the pta-ack and the aceA/aceB promoter regions, and deletion and mutation studies revealed in both regions two binding motifs each consisting of tandem A/C/TG4-6T/C or AC4-5A/G/T stretches separated by four or five arbitrary nucleotides. Our data indicate that RamA represents a novel LuxR-type transcriptional activator of genes involved in acetate metabolism of C. glutamicum.

scholarly journals Physiological Ecology of Stenoxybacter acetivorans, an Obligate Microaerophile in Termite Guts

2007 ◽  
Vol 73 (21) ◽  
pp. 6829-6841 ◽  
Author(s):  
John T. Wertz ◽  
John A. Breznak
Keyword(s):  
Isocitrate Lyase ◽  
Tricarboxylic Acid Cycle ◽  
Glyoxylate Cycle ◽  
Reticulitermes Flavipes ◽  
Peripheral Region ◽  
Malate Synthase ◽  
Rrna Gene ◽  
Potential Contribution ◽  
Cell Extracts

ABSTRACT Stenoxybacter acetivorans is a newly described, obligately microaerophilic β-proteobacterium that is abundant in the acetate-rich hindgut of Reticulitermes. Here we tested the hypotheses that cells are located in the hypoxic, peripheral region of Reticulitermes flavipes hindguts and use acetate to fuel their O2-consuming respiratory activity in situ. Physical fractionation of R. flavipes guts, followed by limited-cycle PCR with S. acetivorans-specific 16S rRNA gene primers, indicated that cells of this organism were indeed located primarily among the microbiota colonizing the hindgut wall. Likewise, reverse transcriptase PCR of hindgut RNA revealed S. acetivorans-specific transcripts for acetate-activating enzymes that were also found in cell extracts (acetate kinase and phosphotransacetylase), as well as transcripts of ccoN, which encodes the O2-reducing subunit of high-affinity cbb 3-type cytochrome oxidases. However, S. acetivorans strains did not possess typical enzymes of the glyoxylate cycle (isocitrate lyase and malate synthase A), suggesting that they may use an alternate pathway to replenish tricarboxylic acid cycle intermediates or they obtain such compounds (or their precursors) in situ. Respirometric measurements indicated that much of the O2 consumption by R. flavipes worker larvae was attributable to their guts, and the potential contribution of S. acetivorans to O2 consumption by extracted guts was about 0.2%, a value similar to that obtained for other hindgut bacteria examined. Similar measurements obtained with guts of larvae prefed diets to disrupt major members of the hindgut microbiota implied that most of the O2 consumption observed with extracted guts was attributable to protozoans, a group of microbes long thought to be “strict anaerobes.”

STUDIES ON RUMEN COLIFORM ORGANISMS: II. UTILIZATION OF ACETATE BY ESCHERICHIA COLI 64 ISOLATED FROM THE RUMEN FLUID OF A COW FED ALFALFA HAY

1967 ◽  
Vol 47 (3) ◽  
pp. 199-209 ◽  
Author(s):  
C. R. Krishnamurti ◽  
L. W. McElroy
Keyword(s):  
Sodium Acetate ◽  
Isocitrate Lyase ◽  
Protein Hydrolysate ◽  
Rumen Fluid ◽  
Glyoxylate Cycle ◽  
Malate Synthase ◽  
E Coli ◽  
Spectrophotometric Methods ◽  
Acetate Medium ◽  
The Glyoxylate Cycle

When cells of E. coli 64 were harvested in their exponential phase of growth in an acetate medium and incubated aerobically with sodium acetate-2-C14, about 33% of the label appeared in CO2 after 1 hr. Of the radioactivity in the cells, 72% was recovered in the protein hydrolysate, 8% in the nucleic acid, 6% in the lipid and 14% in the ethanol-soluble fractions. The radioactivity in the protein hydrolysate of cells incubated with sodium acetate-2-C14 was approximately 20 times that in the hydrolysate of cells incubated with C14O2 as the carbon source. By spectrophotometric methods, it was demonstrated that cell-free extracts of cells grown on acetate contained acetate kinase and phosphate acetyltransferase, plus, as demonstrated by spectrophotometric and isotopic methods, isocitrate lyase and malate synthase which are characteristic of the glyoxylate cycle. The enzymes of the glyoxylate cycle could not be demonstrated in cell-free extracts of E. coli 64 grown on glucose under either aerobic or anaerobic conditions. Possible functions that E. coli 64 may have in the maintenance of anaerobiosis in the rumen and utilization of acetate through the glyoxylate pathway are discussed.

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