Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The preparative scale kinetic resolution of racemic aldols 1-4 using aldolase antibodies 38C2 (Aldrich no. 47995-0) and 84G3 (Aldrich no. 52785-8) is described. These reactions use a biphasic aqueous/organic solvent system that allows the catalyst to be reused. Reaction scales range from miligrams to grams, with 0.0086 to 0.12 mol% of antibody binding sites. Because antibodies 38C2 and 84G3 have opposite enantioselectivities, both aldol product enantiomers are accessible by kinetic resolution.
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PMID:An efficient benchtop system for multigram-scale kinetic resolutions using aldolase antibodies. 1098 25

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.
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PMID:Nonessentiality of boron in fungi and the nature of its toxicity. 1665 56

In addition to its roles in sugar metabolism, fructose-1,6-bisphosphate aldolase (aldolase) has been implicated in cellular functions independent from these roles, termed "moonlighting functions." These moonlighting functions likely involve the known aldolase-actin interaction, as many proteins with which aldolase interacts are involved in actin-dependent processes. Specifically, aldolase interacts both in vitro and in cells with Wiskott-Aldrich Syndrome Protein (WASP), a protein involved in controlling actin dynamics, yet the function of this interaction remains unknown. Here, the effect of aldolase on WASP-dependent processes in vitro and in cells is investigated. Aldolase inhibits WASP/Arp2/3-dependent actin polymerization in vitro. In cells, knockdown of aldolase results in a decreased rate of cell motility and cell spreading, two WASP-dependent processes. Expression of exogenous aldolase rescues these defects. Whether these effects of aldolase on WASP-dependent processes were due to aldolase catalysis or moonlighting functions is tested using aldolase variants defective in either catalytic or actin-binding activity. While the actin-binding deficient aldolase variant is unable to inhibit actin polymerization in vitro and is unable to rescue cell motility defects in cells, the catalytically inactive aldolase is able to perform these functions, providing evidence that aldolase moonlighting plays a role in WASP-mediated processes.
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PMID:Aldolase sequesters WASP and affects WASP/Arp2/3-stimulated actin dynamics. 2349 10