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)
AN INVESTIGATION
WAS
UNDERTAKEN TO DETERMINE WHETHER ANY OF THE FOLLOWING FUNGI HAD A REQUIREMENT FOR BORON (B): Saccharomyces cerevisiae, Aspergillus niger, Neurospora crassa, and Penicillium chrysogenum. Boron was unessential, and hence a study was made of the concentrations of B that reduced the growth of S. cerevisiae and P. chrysogenum and the mode of action of the B toxicity. Fifty and 4000 mg B/liter, respectively, significantly (5% level) reduced the growth of the latter 2 species.In both, glycolysis appeared to be inhibited by toxic levels of B, since the cells accumulated fructose-1,6-diP and ADP, but were low in glyceraldehyde-3-P and ATP. With S. cerevisiae growing on glucose, 150 mg B/liter significantly reduced CO(2) evolution. When glyceraldehyde was substituted for glucose, CO(2) evolution and O(2) consumption were unaffected by this level of B.Aldolase was suspected of being inhibited by high B, and this was confirmed using a crude
aldolase
extract from S. cerevisiae and purified rabbit muscle
aldolase
. The inhibition of
aldolase
by B was uncompetitive.With
aldolase
activity being reduced by toxic levels of B, the fungi were apparently unable to utilize carbohydrates at a rate sufficient to maintain the metabolic processes involved in growth and reproduction.
...
PMID:Nonessentiality of boron in fungi and the nature of its toxicity. 1665 56
The glycolytic enzyme fructose 1,6-(bis)phosphate
aldolase
(
aldolase
) is not only required for efficient utilization of glucose and fructose, but also for cytoskeletal functions like cytokinesis and cell motility. These differing roles are mediated by distinct and discrete binding interactions with
aldolase
's many binding partners, including actin filaments,
Wiskott-Aldrich Syndrome protein
(
WASP
), and Sorting Nexin 9 (SNX9). How these interactions are coordinated on the
aldolase
homotetramer of 160 kDa is unclear. In this study, the catalytic activity of wild-type
aldolase
is measured in the presence of actin filaments, and a
WASP
-derived peptide that binds to
aldolase
, or both. No appreciable changes in k
cat
or K
m
values are seen. Then,
aldolase
variants with substitutions targeting the tryptophan-binding pocket for
WASP
and SNX9 are created and perturbation of actin filament-,
WASP
peptide-, and SNX9 peptide-binding are assessed. Those that negatively impacted binding did not show an impact on
aldolase
catalysis. These results suggest that
aldolase
can engage in catalysis while simultaneously interacting with cytoskeletal machinery. This article is protected by copyright. All rights reserved.
...
PMID:Actin Filament- and Wiskott-Aldrich Syndrome Protein-Binding Sites on Fructose-1,6-bisphosphate Aldolase are Functionally Distinct from the Active Site. 3321 Apr 55
