Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.9.3.1 (cytochrome oxidase)
 8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Bacteria engineered with the gene (vgb) encoding Vitreoscilla hemoglobin (VHb) typically produce more protein than unengineered cells, and it has generally been assumed that VHb is responsible for this effect. Here, using matched strains of E. coli that bear a recombinant alpha-amylase gene (MK57) or the alpha-amylase gene and vgb (MK79), we provide evidence supporting this assumption. Sodium nitrite (which is known to inhibit heme proteins) was tested over a range of concentrations regarding effects on growth, alpha-amylase production, respiration, and VHb function in MK57 and MK79. Nitrite concentrations were identified at which respiration of cell membranes was inhibited only slightly and to approximately equal degrees in both strains, while whole cell respiration was inhibited to a greater extent and about twice as much in MK79 as MK57. This suggests that these concentrations inhibit VHb while having a much smaller effect on cytochrome oxidase. Direct measurements of VHb showed, in fact, that the same nitrite concentrations greatly decreased the levels of active (ferrous) and, to a somewhat lesser extent, total (ferrous plus ferric) VHb in MK79. Finally, these same nitrite concentrations reversed the advantage regarding alpha-amylase production of MK79 over MK57 seen at 0 mM nitrite, linking the presence of active VHb with the increase in alpha-amylase production.
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PMID:Nitrite inhibition of Vitreoscilla hemoglobin (VHb) in recombinant E. coli: direct evidence that VHb enhances recombinant protein production. 1110 16

Genetically engineering the heterologous bacterial host with the gene (vgb) encoding Vitreoscilla haemoglobin (VHb) has been found to provide typical advantages in growth and production, and it has generally been assumed that VHb is responsible for this effect. Here, using matched strains of Escherichia coli that bear a recombinant R-amylase gene (MK57) or the R-amylase gene and vgb (MK79), we examined this assumption. Menadione, which is known to oxidize haem proteins, was tested over a range of concentrations for its effects on growth, R-amylase production, respiration and VHb function in MK57 and MK79. Active VHb accumulated, and VHb was oxidized to the inactive ferric form with the use of menadione at the concentrations of 0.5-10 mM; concentrations that had a much smaller effect on cytochrome oxidase. This decrease in active VHb in strain MK79 was correlated with a reverse in the advantage regarding R-amylase production of MK79 over MK57 seen at a menadione concentration of 0 mM, thus linking the presence of active VHb with the increase in R-amylase production. It is concluded that vgb, and not any other Vitreoscilla DNA sequences on plasmid pMK79, is the source of the advantages in both the growth and product production of alpha-amylase in this system.
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PMID:Menadione knocks out Vitreoscilla haemoglobin (VHb): the current evidence for the role of VHb in recombinant Escherichia coli. 1265 36

The ability of the synthesized compounds of germanium with bioligands to affect the biosynthesis and activity of alpha-amylase and alpha-L-rhamnosidase has been studied. It was established the most complexes tested induced biosyntheis of alpha-amylase of Bacillus subtilis 147 (119-252%) with the exception of Pam (Pyracetam) and II (Ge-nicotinic-citric acid). At the same time the biosynthesis of alpha-amylase of Bacillus licheniformis 234 and alpha-L-rhamnosidase of Penicillium commune was inhibited by a number of synthesized compounds. The complexes IV (Ge-malonic acid) and VIII (Ge-nicotinamide-malonic acid) did not exert any effect on the biosynthesis of alpha-amylase however complex IV stimulated alpha-L-rhamnosidase biosynthesis on the 3rd day of producer cultivation. The study of influence of the studied germanium compounds on the activity of alpha-amylase and alpha-L-rhamnosidase gives every reason to suppose that they are the inhibitors of the above-mentioned enzymes.
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PMID:[The influence of coordinational germanium compounds on the activity of glycosidases]. 1768 26