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

It has been proposed recently that translation of fructose-1,6-diphosphate aldolase of the malaria parasite Plasmodium falciparum is initiated at a UAG codon, both in the parasite and in a rabbit reticulocyte cell-free translation system. We have introduced mutations around that UAG codon and find that cell-free expression of a construct encoding an AUG in this position results in a slightly larger translation product. The translation product of the construct encoding the UAG codon is of the same apparent molecular weight as the products obtained from two other constructs; one in which the UAG is replaced by AAG, and one in which nucleotides upstream from a second AUG codon are deleted. Thus we show that translation is not initiated at the UAG and conclude that synthesis of aldolase in the parasite starts at an AUG, provided after splicing of pre-mRNA.
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PMID:In vitro translation of Plasmodium falciparum aldolase is not initiated at an unusual site. 191 82

In vitro chaperone-like activity of the acute-phase component and plasma drug transporter human alpha(1)-acid glycoprotein (AAG) has been shown for the first time. AAG suppressed thermal aggregation of a variety of unrelated enzymatic (e.g., aldolase, catalase, enolase, carbonic anhydrase) and non-enzymatic proteins (beta-lactoglobulin, ovotransferrin) and it also prevented dithiothreitol induced aggregation of insulin. The anti-aggregation ability of AAG was abolished/reduced upon drug binding suggesting that protein-protein interactions established between the lipocalin beta-barrel fold of AAG and hydrophobic surfaces of the stressed proteins are involved in the chaperone-like activity. The results shed some light on the possible biological function of this enigmatic protein and suggest that besides haptoglobin, clusterin, fibrinogen and alpha(2)-macroglobulin AAG can be considered as a novel member of the extracellular molecular chaperones found in human body fluids.
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PMID:Chaperone-like activity of the acute-phase component human serum alpha 1-acid glycoprotein: inhibition of thermal- and chemical-induced aggregation of various proteins. 2002 2