Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:4.1.2.13 (
aldolase
)
3,461
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Aspergillus nidulans was completely devoid of fruit bodies when grown on manganese deficient cultures. This result was shown earlier to be due to a lack of alpha-1,3
glucan
in the cell wall. Several enzymes of carbon and nitrogen metabolism were investigated in an attempt to explain the absence of this reserve material. Synthesis of glucose-6-phosphate dehydrogenase, phosphoglucoisomerase and
aldolase
, were not strongly affected by manganese deficiency. However, phosphoglucomutase showed only 60% of the activity of the control cultures and it was argued that this was connected with the low amounts of alpha-1,3
glucan
synthesized. Malate dehydrogenase was the enzyme the least affected by manganese deficiency and the two to threefold higher activity measured after glucose depletion might indicate the induction of the glyoxylate cycle. An impaired glutamine synthetase could explain the increase in activity observed for NAD-glutamine dehydrogenase.
...
PMID:Sexual differentiation in Aspergillus nidulans: the requirement for manganese and the correlation between phosphoglucomutase and the synthesis of reserve material. 17 48
The composition of
glucan
-associated proteins (GAP) in the cell wall of Candida albicans was strongly affected by treatment with a sub-MIC yet beta-
glucan
synthesis inhibitory concentration (0.01 microg/ml) of FK463 (micafungin). Namely, a decrease in enzymes of glucose metabolism (mostly enolase and a novel 40 kDaltons component, here identified as the enzyme fructose-1,6-biphosphate
aldolase
) was observed, and this was coupled with an increase in two beta1-3 exo-glucanase isoforms (34 and 44 kDa, respectively). No GAP changes were detected in the same strain of the fungus made resistant to the drug, attesting to the specificity of the observed cell wall protein modulation. In addition, GAP changes were accompanied by marked ultrastructural alterations upon treatment with the sub-MIC dose of the drug, the majority of which was an aberrant cell surface morphology and a derangement of the normal layering of the cell wall. Our data demonstrate that sub-MIC doses of micafungin do critically affect not only the beta-
glucan
synthetic machinery but also protein composition and the whole cell wall structure of Candida albicans.
...
PMID:Glucan-associated protein modulations and ultrastructural changes of the cell wall in Candida albicans treated with micafungin, a water-soluble, lipopeptide antimycotic. 1616 21
The echinocandins (e.g., caspofungin) are a relatively new class of antifungal drugs that function by inhibiting the synthesis of beta-1,3-
glucan
in the cell wall and thus lead to lysis of the cell. In this work the effect of caspofungin on the release of peptides from non-growing cells of the yeast Candida albicans that had been exposed to the drug was monitored. Exposure to 0.19 mug/ml caspofungin resulted in the release of amino acids from cells and of both small and large molecular weight proteins as demonstrated by 1- and 2-dimensional gel electrophoresis. Matrix-assisted laser desorption/ionization-time of flight-mass spectrometry (MALDI-ToF) mass spectrometry was employed to identify a number of escaped peptides that were found to have increased in intensity upon exposure to the drug. A number of wall-associated proteins (e.g., phosphoglycerate kinase) and a number of glycolytic enzymes (phosphoglycerate mutase 1,
fructose-bisphosphate aldolase
) were identified. Importantly, several released proteins (e.g., pyruvate kinase, enolase 1, phosphoglycerate mutase, glyceraldehydes 3-phosphate dehydrogenase, fructose bisphosphate aldolase and alcohol dehydrogenase 1) are highly immunogenic in nature. The results presented here demonstrate that non-growing C. albicans cells are susceptible to the effect of caspofungin and that the caspofungin-mediated release of proteins from such cells could lead to a stronger immune response in vivo. This report illustrates that, in addition to hampering cell wall synthesis, caspofungin may also interfere with the permeability of the fungal cell wall.
...
PMID:Proteomic analysis of proteins released from growth-arrested Candida albicans following exposure to caspofungin. 2039 51