Gene expression enzymes

Gene Expression Enzyme Activity Both Are Regulated... 

Molecular/Cellular metabolism gene expression enzyme induction immune function cellular alteration... 

Goodridge, A.G. (1987). Dietary regulation of gene expression enzymes involved in carbohydrate and lipid metabolism. Ann. Rev. Nutr. 1 157— 185. 

As noted earlier, the velocity of any enzyme-catalyzed reaction is dependent upon the amount of effective enzyme present. Enzyme biosynthesis, like that of all proteins, is under genetic control, a long-term process. Biosynthesis of enzymes may be increased or decreased at the genome level. Various hormones can activate or repress the mechanisms controlling gene expression. Enzyme levels are the result of the balance between synthesis and degradation. This enzyme turnover may be altered by diverse physiological conditions, by hormone effects, and by the level of metabolites. 

Zinc (Zn +) is the second most abundant metal ion after iron in the human body, and plays critical roles in regulating gene expression, enzyme regulation, and neurotransmission [90]. Zn + is also known to be responsible for the formation of amyloid plaques during the onset of Alzheimer s disease [91], At present, there is considerable interest in the development of Zn +-selective luminescence chemosensors as bioimaging probes [92, 93],... 

Promoter recognition by a specific pollutant followed by gene expression, enzyme synthesis and catalytic activity. 

In contrast to the harmful biogenic amines, the polyamines putrescene, spermidine and spermine are necessary for optimal growth and function of cells. They are involved in DNA, RNA and protein synthesis, regulation of gene expression, enzyme activity, cell proliferation and cell signaUtng. 

Bioengineering enzyme production (including gene expression, enzyme purification, and formulation), fermentation, membrane technology, process systems engineering. 

For the bioinformatician the emphasis lies on how a gene expresses a protein -an enzyme - that catalyzes a biochemical reaction (Figure 10.3-13). 

Puromycin. Puromycin (19), elaborated by S. alboniger (1—4), inhibits protein synthesis by replacing aminoacyl-tRNA at the A-site of peptidyltransferase (48,49). Photosensitive analogues of (19) have been used to label the A-site proteins of peptidyltransferase and tRNA (30). Compound (19), and its carbocycHc analogue have been used to study the accumulation of glycoprotein-derived free sialooligosaccharides, accumulation of mRNA, methylase activity, enzyme transport, rat embryo development, the acceptor site of human placental 80S ribosomes, and gene expression in mammalian cells (51—60). 

Tanahashi, H., etal. (1990). Photoprotein aequorin use as a reporter enzyme in studying gene expression in mammalian cells. Gene 96 249-255. 

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