Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.1.1 (hexokinase)
 5,274 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of chronic intake of di(2-ethylhexyl)phthalate (DEHP) on the main intermediate glycolytic metabolites in liver and gastrocnemius muscle were investigated in experimental animals. Male Wistar rats (90-100 g) were fed for 21 days either with a standard chow or the same diet supplemented with 2% (w/w) of DEHP. The DEHP-fed rats had an altered in vivo glucose tolerance associated with abnormal glucose intermediate metabolite contents in liver and skeletal muscle. In these rats, the hepatic content of glucose-6-phosphate (G-6-P), fructose-6-phosphate, pyruvate, lactate, glucose-1-phosphate and glycogen decreased. At the same time, the G-6-P content decreased while the pyruvate and lactate levels increased in skeletal muscle. These data, along with the high plasma glucose concentration and the normal lactate blood levels of this group, could indicate that DEHP-fed rats could present a deficiency in muscle glucose and lactate transport, a reduction of the flux through muscle hexokinase and hepatic glucokinase, and a reduction in glycogen synth-
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PMID:Dietary di(2-ethylhexyl)phthalate-impaired glucose metabolism in experimental animals. 1701 6

Static fluorescence measurements from the protein Tryptophan (Trp) residues and circular dichroism (CD) spectroscopy were used to investigate changes on the tertiary and secondary structures of the protein bovine serum albumin (BSA) and the dimeric enzyme hexokinase (HK) type PII from yeast, entrapped in reversed micelles (RMs). The latter were obtained from the amphiphilic AOT (sodium bis-2-ethylhexyl sulfosuccinate) in n-hexane, at several water to surfactant ratios, W. BSA and HK were found to be anchored at the RM interface in close contact with the surfactant layer, regardless of the size of the waterpool. For BSA, such interaction promotes partial protein unfolding, according to CD data that showed a decrease in the content of helical structure from 66% in a buffer solution to 48% in the micellar moiety. When urea was present in the micelle, further loss in helical structure occurred, thus indicating that the combined effect (micellar environment and urea) altered the BSA conformation to a greater extent than did RM or urea alone. Interestingly, Trps probed the same environment in the micelle, regardless of the presence of urea, but the fluorescence was quenched to a higher extent with urea. Thus, the fluorofore emission must have been affected either by the direct interaction of urea or by indirect exchange of water structure caused by urea interacting with water and the micellar interface. Both mechanisms might be of relevance in the solvation properties nearby the Trps. For HK, an association between the enzyme and the micelle interface was indicated in the CD spectra, which exhibited a randomized structure upon interaction, whatever the RM droplet size. The urea addition to the micelle water pool did not cause further impact on the HK conformation. In addition, the influence of urea at the RM interface was not sensed by the exposed tryptophans of the enzyme, unlike the results for BSA.
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PMID:The influence of urea on the structure of proteins in reversed micelles. 1703 50