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Results for “ALCALIGENES”

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At least 847 records · Page 47Linked to original sources
PubMed1996

Site-directed mutagenesis of azurin from Pseudomonas aeruginosa enhances the formation of an electron-transfer complex with a copper-containing nitrite reductase from Alcaligenes faecalis S-6.

Kinetic analysis of electron transfer between azurin from Pseudomonas aeruginosa and copper-containing nitrite reductase (NIR) from Akaligenes faecalis S-6 was carried out to investigate the specificity of electron transfer between copper-containing proteins. Apparent values of kcat and Km of NIR for azurin were 300-fold smaller and 172-fold larger than those for the physiological redox partner, pseudoazurin from A. faecalis S-6, respectively, suggesting that the electron transfer between azurin and NIR was less specific than that between pseudoazurin and NIR. One of the major differences in 3-D structure between these redox proteins, azurin and pseudoazurin, is the absence and presence of lysine residues near their type 1 copper sites, respectively. Three mutated azurins, D11K, P36K, and D11K/P36K, were constructed to evaluate the importance of lysine residues in the interaction with NIR. The redox potentials of D11K, P36K, and D11K/P36K azurins were higher than that of wild-type azurin by 48, 7, and 55 mV, respectively. As suggested by the increase in the redox potential, kinetic analysis of electron transfer revealed reduced ability of electron transfer in the mutated azurins. On the other hand, although each of the single mutations caused modest effects on the decrease in the Km value, the simultaneous mutations of D11K and P36K caused significant decrease in the Km value when compared to that for wild-type azurin. These results suggest that the introduction of two lysine residues into azurin facilitated docking to NIR.

Alcaligenes↗
PubMed1979

Mutations altering the catalytic activity of a plant-type ribulose biphosphate carboxylase/oxygenase in Alcaligenes eutrophus.

Use of a bacterial system has allowed the isolation of several mutationally altered species of ribulose-1,5-bisphosphate carboxylase/oxygenase having a wide range of catalytic activities. Biochemical and serological techniques were used to classify the mutant strains into three groups: (1) no detectable ribulose-1,5-bisphosphate carboxylase/oxygenase protein present (both subunits missing); (2) mutant strains having ribulose-1,5-bisphosphate carboxylase/oxygenases with lowered specific activities; and (3) mutant strains producing large quantities of catalytically inactive ribulose-1,5-bisphosphate carboxylase/oxygenase.

Alcaligenes↗
PubMed2005

Effects of paraoxon and ethylparathion on choline oxidase from Alcaligenes species: inhibition and denaturation.

The kinetics and thermodynamics of the effects of paraoxon (POX) and ethylparathion (EPA) on choline oxidase (ChOx) were studied. Lineweaver-Burk plots of initial velocity data showed a parallel pattern indicating uncompetitive inhibition versus choline. The inhibition constant (K(I)) obtained from the secondary plots for POX and EPA were 0.14+/-0.01 and 0.48+/-0.05 mM, respectively, suggesting that POX is a more potent inhibitor of ChOx than EPA. UV absorption was used to monitor the denaturation of ChOx by POX and EPA. A decrease in FAD fluorescence associated with the interaction of POX and EPA with ChOx suggested a tertiary structural change. Interaction of the enzyme molecule with POX or EPA resulted in inhibition and subsequently denaturation of the enzyme. The results indicate that inhibition and denaturation of the enzyme by POX and EPA are linked, but not parallel events, with inhibition occurring at lower concentrations with respect to denaturation. This suggests that the loss of initial velocity of the enzyme is an active site specific effect and not due to global conformational changes induced by the inhibitors.

Alcaligenes↗