Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0040822 (tremor)
 18,428 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The stability of various glycolytic enzymes of human erythrocytes has been studied by the mechanical shaking method. The rate of denaturation apparently followed first order kinetics. The t1/2, the shaking time required to denature 50% of the original activity, for glucose-6-phosphate dehydrogenase, phosphofructokinase, and pyruvate kinase was less than 1 min; that for hexokinase, 6-phosphogluconate dehydrogenase, and monophosphoglyceromutase was between 2 and 13 min; that for all the other enzymes was more than 30 min. Since the t1/2 value for each enzyme is highly reproducible if the shaking conditions are kept constant, these parameters may be used as an indicator of protein stability in solution. The mechanical denaturation method may also be used to remove unstable components from a mixture of proteins with different stabilities.
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PMID:Stability of glycolytic enzymes of human erythrocytes. 83 47

Rat liver enzymes were used to study the relationship between their in vivo half-lives and their apparent hydrophobicity or their resistance to inactivation by mechanical shaking. The apparent hydrophobicity of these enzymes, measured as the percent of the protein recovered from an octyl-Sepharose column, is correlated with their known half-lives (r = 0.75, P less than 0.01). The presence of specific ligands which are known to increase compactness by impeding unfolding of proteins decreased the apparent hydrophobicity of fructose-1,6-bisphosphatase, glucose-6-phosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, and pyruvate kinase. Resistance of enzymes to inactivation by mechanical shaking correlated well with their in vivo half-lives (r = 0.90, P less than 0.01). When the shaking experiments were done in the presence of substrates, fructose-1,6-bisphosphatase, glucose-6-phosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase were protected from inactivation.
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PMID:Protein hydrophobicity and stability support the thermodynamic theory of protein degradation. 633 12

Tsukada, Yoji (Kyoto University, Kyoto, Japan), Tsunetake Sugimori, Kazutami Imai, and Hideo Katagiri. Action of cycloheximide on Zygosaccharomyces soja. J. Bacteriol. 83:70-75. 1962.-Cycloheximide is known to inhibit the growth of some species of Saccharomyces and other fungi. A new type of action of this antibiotic, with Zygosaccharomyces soja as the test organism, is described in this paper. Growth of Z. soja was completely inhibited under aerobic conditions by cycloheximide in concentrations of more than 5 mug per ml of culture solution. Continued shaking of the culture for more than 96 hr in the presence of an inhibitory amount of cycloheximide restored growth, accompanied by the excretion of riboflavin to the extent of 30 mug per ml of culture solution. In the cells recovering from cycloheximide inhibition, the type of glucose metabolism differed from that in the mother strain; a respiratory quotient of 4 with the mother strain fell to 1 in the progeny. Glucose metabolism (O(2) uptake and CO(2) evolution) by resting cells was investigated, and it was concluded that inhibition of glycolysis was not significant. This was verified by comparing various dehydrogenase activities in the cell-free extract. There were essentially no differences between riboflavin-forming and nonriboflavin-forming cells. The presence of the hexose monophosphate shunt was deduced from the fact that glucose-6-phosphate dehydrogenase activity was the strongest of the various dehydrogenase activities.
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PMID:A ction of cycloheximide on Zygosaccharomyces soja. 1392 90

Genes of zwf1 and zwf2 encode two isozymes of glucose-6-phosphate dehydrogenase (G6PDH) of Streptomyces, respectively. G6PDH is the first enzyme in the oxidative pentose phosphate pathway (PPP) and the key enzyme for NADPH generation. Based on thermal sensitive plasmid pKC1139, a recombinant plasmid pKC1139-zwf2' was constructed and verified with restriction enzyme digestion. The plasmid pKC1139-zwf2' was electropolated into competent Streptomyces rimosus M4018 cells after it was demethylated by E. coli GM2929. Transformants grown on Tryptone Soya Agar (TSA) plate containing 500 ug/mL apramycin were selected, and identified using dot hybridization analysis and PCR amplification with apramycin resistant gene as primers. A positive clone was then selected and designated M4018-delta zwf2. With parent strain S. rimosus M4018 as control, mutant M4018-delta zwf2 was cultured in shaking flask. Specific acitivity of G6PDH of M4018-delta zwf2 was only half of that of parent strain whereas yield of oxytetracycline (OTC) of mutant was 27% higher to the mutant had a similar biomass profileto that of the control biosynthesis started when the growth entered stationary phase on the 4th day. However, specific oxytetracycline production of mutant was 31% higher than that of the parent strain, indicating that zwf2 disruption could enhance oxytetracycline biosynthesis in S. rimosus M4018-delta zwf2.
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PMID:[Disruption of zwf2 gene to improve oxytetraclyline biosynthesis in Streptomyces rimosus M4018]. 1833 71