scholarly journals Inhibitory Effects of Epipolythiodioxopiperazine Fungal Metabolites on Isocitrate Lyase in the Glyoxylate Cycle of Candida albicans

Marine Drugs ◽  
2021 ◽  
Vol 19 (6) ◽  
pp. 295
Author(s):  
Ji-Yeon Hwang ◽  
Beomkoo Chung ◽  
Oh-Seok Kwon ◽  
Sung Chul Park ◽  
Eunji Cho ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Inhibitory Concentration ◽  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
Spectroscopic Techniques ◽  
Fungal Metabolites ◽  
Inhibitory Effects ◽  
Polymerase Chain ◽  
Reported Data ◽  
The Glyoxylate Cycle

Four epipolythiodioxopiperazine fungal metabolites (1–4) isolated from the sponge-derived Aspergillus quadrilineatus FJJ093 were evaluated for their capacity to inhibit isocitrate lyase (ICL) in the glyoxylate cycle of Candida albicans. The structures of these compounds were elucidated using spectroscopic techniques and comparisons with previously reported data. We found secoemestrin C (1) (an epitetrathiodioxopiperazine derivative) to be a potent ICL inhibitor, with an inhibitory concentration of 4.77 ± 0.08 μM. Phenotypic analyses of ICL-deletion mutants via growth assays with acetate as the sole carbon source demonstrated that secoemestrin C (1) inhibited C. albicans ICL. Semi-quantitative reverse-transcription polymerase chain reaction analyses indicated that secoemestrin C (1) inhibits ICL mRNA expression in C. albicans under C2-assimilating conditions.

scholarly journals Inhibitory Effects of Diketopiperazines from Marine-Derived Streptomyces puniceus on the Isocitrate Lyase of Candida albicans

Molecules ◽  
2019 ◽  
Vol 24 (11) ◽  
pp. 2111 ◽  
Author(s):  
Heegyu Kim ◽  
Ji-Yeon Hwang ◽  
Jongheon Shin ◽  
Ki-Bong Oh
Keyword(s):  
Candida Albicans ◽  
Cyclic Peptides ◽  
Inhibitory Concentration ◽  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
Malate Synthase ◽  
Wild Type ◽  
Inhibitory Effects ◽  
Reported Data ◽  
The Glyoxylate Cycle

The glyoxylate cycle is a sequence of anaplerotic reactions catalyzed by the key enzymes isocitrate lyase (ICL) and malate synthase, and plays an important role in the pathogenesis of microorganisms during infection. An icl-deletion mutant of Candida albicans exhibited reduced virulence in mice compared with the wild type. Five diketopiperazines, which are small and stable cyclic peptides, isolated from the marine-derived Streptomyces puniceus Act1085, were evaluated for their inhibitory effects on C. albicans ICL. The structures of these compounds were elucidated based on spectroscopic data and comparisons with previously reported data. Cyclo(L-Phe-L-Val) was identified as a potent ICL inhibitor, with a half maximal inhibitory concentration of 27 μg/mL. Based on the growth phenotype of the icl-deletion mutants and icl expression analyses, we demonstrated that cyclo(L-Phe-L-Val) inhibits the gene transcription of ICL in C. albicans under C2-carbon-utilizing conditions.

scholarly journals The Glyoxylate Cycle Is Involved in White-Opaque Switching in Candida albicans

2021 ◽  
Vol 7 (7) ◽  
pp. 502
Author(s):  
Susana Hidalgo Vico ◽  
Daniel Prieto ◽  
Rebeca Alonso Monge ◽  
Elvira Román ◽  
Jesús Pla
Keyword(s):  
Transcription Factor ◽  
Candida Albicans ◽  
Gastrointestinal Tract ◽  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
Carbon Sources ◽  
Glyoxylate Shunt ◽  
Phenotypic Analysis ◽  
Altered Metabolism ◽  
The Glyoxylate Cycle

Candida albicans is a commensal yeast that inhabits the gastrointestinal tract of humans. The master regulator of the white-opaque transition WOR1 has been implicated in the adaptation to this commensal status. A proteomic analysis of cells overexpressing this transcription factor (WOR1OE) suggested an altered metabolism of carbon sources and a phenotypic analysis confirmed this alteration. The WOR1OE cells are deficient in using trehalose and xylose and are unable to use 2C sources, which is consistent with a reduction in the amount of Icl1, the isocitrate lyase enzyme. The icl1Δ/Δ mutants overexpressing WOR1 are deficient in the production of phloxine B positive cells, a main characteristic of opaque cells, a phenotype also observed in mating type hemizygous mtla1Δ icl1Δ/Δ cells, suggesting the involvement of Icl1 in the adaptation to the commensal state. In fact, icl1Δ/Δ cells have reduced fitness in mouse gastrointestinal tract as compared with essentially isogenic heterozygous ICL1/icl1Δ, but overproduction of WOR1 in an icl1Δ/Δ mutant does not restore fitness. These results implicate the glyoxylate shunt in the adaptation to commensalism of C. albicans by mechanisms that are partially independent of WOR1.

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.

Acetate metabolism in Escherichia coli

1978 ◽  
Vol 24 (2) ◽  
pp. 149-153 ◽  
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.

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

scholarly journals Synthesis, Characterization of Some Novel Benzimidazole Derivatives of 1-Bromo-2,4-dinitrobenzene and Their Antifungal Activities

2011 ◽  
Vol 8 (s1) ◽  
pp. S85-S90
Author(s):  
Abbas Ahmadi ◽  
Babak Nahri-Niknafs
Keyword(s):  
Biological Activity ◽  
Candida Albicans ◽  
Candida Glabrata ◽  
Inhibitory Concentration ◽  
Candida Krusei ◽  
Benzimidazole Derivatives ◽  
Spectroscopic Techniques ◽  
Antifungal Activities ◽  
Derivatives Of

Six novel benzimidazole derivatives, 5-nitro-2-phenyl -1-ethyl benzimidazol (5), 2- (p-bromophenyl)- 5-nitro- 1-ethyl benzimidazol (6), 2- (p-bromophenyl-5-nitro-1–cyclopentyl benzimidazol (7), 2- (p-bromophenyl) -5-nitro-1-cyclopentyl benzimidazol (8), 5-amino-2-(p-bromophenyl)-1-ethylbenzimidazol (9) and 5-amino-2-(p-bromophenyl)-1-cyclopentyl benzimidazol (10) were synthesized. The structures of all the synthesized compounds were elucidated by using elemental analysis and different spectroscopic techniques (IR, NMR and mass spectroscopy). Some of these compounds showed potential antifungal activities. The biological activity of these compounds as fungicides was tested against Candida albicans, patient isolate Candida glabrata and Candida krusei. The biological activity of four compounds was found to be comparable to that of the commercially available fungicides with a minimum inhibitory concentration of 12.5 µg/mL.

scholarly journals Suvanine Sesterterpenes from a Tropical Sponge Coscinoderma sp. Inhibit Isocitrate Lyase in the Glyoxylate Cycle

Marine Drugs ◽  
2014 ◽  
Vol 12 (10) ◽  
pp. 5148-5159 ◽  
Author(s):  
So-Hyoung Lee ◽  
Tae Won ◽  
Heegyu Kim ◽  
Chan-Hong Ahn ◽  
Jongheon Shin ◽  
...  
Keyword(s):  
Isocitrate Lyase ◽  
Glyoxylate Cycle ◽  
The Glyoxylate Cycle

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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