Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0034186 (pyelonephritis)
 6,144 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

As many as 159 patients with chronic pyelonephritis and 100 those with glomerulonephritis residing in ecologically favourable, and on contaminated territories for 6-8 years after Chernobyl accident, were examined for indices of lipid peroxidation, antioxidant system and energy exchange. The above renal disease were found to be accompanied by a rise in the activity of lipid peroxidation and accumulation of excess of their products in cellular membranes and urine. In the antioxidant system, the activity of NAD-H2-dependent factors and an inhibitor of free radical oxidation of superoxiddismutase tends to decrease. There occur changes in isoenzyme spectrum of lactate and malatedehydrogenases. The above shifts appear to be manifest in those persons having been exposed to low radiation doses. Antioxidants and stabilizers of the biological membranes were shown to be useful in correcting the above metabolic processes.
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PMID:[The metabolic aspects of the sequelae of the accident at the Chernobyl Atomic Electric Power Station in the course of kidney diseases]. 863 Jul 88

Sequence comparisons have implied the presence of genes encoding enzymes of the mevalonate pathway for isopentenyl diphosphate biosynthesis in the gram-positive pathogen Staphylococcus aureus. In this study we showed through genetic disruption experiments that mvaA, which encodes a putative class II 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, is essential for in vitro growth of S. aureus. Supplementation of media with mevalonate permitted isolation of an auxotrophic mvaA null mutant that was attenuated for virulence in a murine hematogenous pyelonephritis infection model. The mvaA gene was cloned from S. aureus DNA and expressed with an N-terminal His tag in Escherichia coli. The encoded protein was affinity purified to apparent homogeneity and was shown to be a class II HMG-CoA reductase, the first class II eubacterial biosynthetic enzyme isolated. Unlike most other HMG-CoA reductases, the S. aureus enzyme exhibits dual coenzyme specificity for NADP(H) and NAD(H), but NADP(H) was the preferred coenzyme. Kinetic parameters were determined for all substrates for all four catalyzed reactions using either NADP(H) or NAD(H). In all instances optimal activity using NAD(H) occurred at a pH one to two units more acidic than that using NADP(H). pH profiles suggested that His378 and Lys263, the apparent cognates of the active-site histidine and lysine of Pseudomonas mevalonii HMG-CoA reductase, function in catalysis and that the general catalytic mechanism is valid for the S. aureus enzyme. Fluvastatin inhibited competitively with HMG-CoA, with a K(i) of 320 microM, over 10(4) higher than that for a class I HMG-CoA reductase. Bacterial class II HMG-CoA reductases thus are potential targets for antibacterial agents directed against multidrug-resistant gram-positive cocci.
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PMID:Essentiality, expression, and characterization of the class II 3-hydroxy-3-methylglutaryl coenzyme A reductase of Staphylococcus aureus. 1096 99