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)

Exposure of foundry workers to mixtures of different heavy metals is a very important toxicological problem. In this paper the estimation of the effects of lead, zinc, and copper on erythrocyte metabolism is presented. Concentrations of copper and zinc at work posts of the group examined did not exceed TLV, while lead concentration was 1.5 to 4 times higher than TLV. Erythrocyte metabolism was measured through activities of such glycolytic pathway enzymes as PFK, PGI, PK, aldolase and G6-PD from the hexose monophosphate pathway. Additionally the free erythrocyte protoporphyrin (FEP) level, D-ALA activity, serum GSH level, 2,3 DPG level in erythrocytes and lactic acid production during a 2-h incubation of red blood cells (RBC) was estimated. The blood-lead level, FEP level, copper concentration in erythrocytes in exposed group were significantly higher than in control group while the zinc level in erythrocytes was significantly lower. Measuring erythrocyte metabolism we showed that the activity of PGI, PFK, aldolase, lactic production and 2,3 DPG levels was significantly higher in the exposed group, probably as a result of anaerobic glycolysis activation.
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PMID:Influence of heavy metal mixtures on erythrocyte metabolism. 234 40

Pyridoxal kinase displays high catalytic activity in the presence of metallothionein. The apoprotein of metallothionein as well as the peptide LYS-CYS-THR-CYS-CYS-ALA exert a strong inhibitory effect upon pyridoxal kinase by sequestering free Zn ions. Several steps intervene in the process of pyridoxal kinase activation, i.e. binding of Zn ions by ATP and interaction of Zn-ATP with the enzyme; but direct interaction between metallothionein and pyridoxal kinase (protein association) could not be detected by emission anisotropy measurements. Since the concentration of free Zn++ in mammalian tissues is lower than 10(-9)M, it is postulated that the concentration of metallothionein regulates the catalytic activity of pyridoxal kinase. The mechanism of reconstitution of the metalloenzyme yeast aldolase in the presence of metallothionein was also investigated.
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PMID:Modulation of the catalytic activity of pyridoxal kinase by metallothionein. 284 38

Alpha-synuclein, a major constituent of Lewy bodies (LBs) in Parkinson's disease (PD), has been implicated to play a critical role in synaptic events, such as neuronal plasticity during development, learning, and degeneration under pathological conditions, although the physiological function of alpha-synuclein has not yet been established. We here present biochemical evidence that recombinant alpha-synuclein has a chaperone-like function against thermal and chemical stress in vitro. In our experiments, alpha-synuclein protected glutathione S-transferase (GST) and aldolase from heat-induced precipitation, and alpha-lactalbumin and bovine serum albumin from dithiothreitol (DTT)-induced precipitation like other molecular chaperones. Moreover, preheating of alpha-synuclein, which is believed to reorganize the molecular surface of alpha-synuclein, increased the chaperone-like activity. Interestingly, in organic solvents, which promotes the formation of secondary structure, alpha-synuclein aggregated more easily than in its native condition, which eventually might abrogate the chaperone-like function of the protein. In addition, alpha-synuclein was also rapidly and significantly precipitated by heat in the presence of Zn2+ in vitro, whereas it was not affected by the presence of Ca2+ or Mg2+. Circular dichroism spectra confirmed that alpha-synuclein underwent conformational change in the presence of Zn2+. Taken together, our data suggest that alpha-synuclein could act as a molecular chaperone, and that the conformational change of the alpha-synuclein could explain the aggregation kinetics of alpha-synuclein, which may be related to the abolishment of the chaperonic-like activity.
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PMID:Structural changes in alpha-synuclein affect its chaperone-like activity in vitro. 1120 70