Properties of 1-phosphofructokinase from Pseudomonas piutida

1977 ◽  
Vol 23 (6) ◽  
pp. 721-725 ◽  
Author(s):  
Sookie S. Bang ◽  
Paul Baumann ◽  
Mark H. Sawyer
Keyword(s):  
Pseudomonas Putida ◽  
Adenosine Triphosphate ◽  
Column Chromatography ◽  
Inhibitory Activity ◽  
Reaction Rate ◽  
Adenosine Monophosphate ◽  
The Other ◽  
Kinetic Properties ◽  
Sephadex Column ◽  
Sigmoidal Kinetics

The 1-phosphofructokinase (1-PFK, EC 2.7.1.56) from Pseudomonas putida was partially purified by a combination of (NH4)2SO4 fractionation and DEAE-Sephadex column chromatography. In its kinetic properties, this enzyme resembled the 1-PFK's from other bacteria. With the substrates fructose-1-phosphate (F-1-P) and adenosine triphosphate (ATP) Michaelis–Menten kinetics were observed, the Km for one substrate being unaffected by a variation in the concentration of the other substrate. At pH 8.0, the Km values for F-1-P and ATP were 1.64 × 10−4 M and 4.08 × 10−4 M, respectively. At fixed concentrations of F-1-P and ATP, an increase in the Mg2+ resulted in sigmoidal kinetics. Activity was inhibited by ATP when the ratio of ATP:Mg2+ was greater than 0.5 suggesting that ATP:2 Mg2+ was the substrate and free ATP was inhibitory. Activity of 1-PFK was stimulated by K+ and to a lesser extent by NH4+ and Na+. The reaction rate was unaffected by 2 mM K2HPO4, pyruvate, phosphoenolpyruvate, adenosine monophosphate, adenosine 3′,5′-cyclic monophosphate, fructose-6-phosphate, glucose-6-phosphate, 6-phosphogluconate, 2-keto-3-deoxy-6-phosphogluconate, or citrate. The results indicated that the 1-PFK from P. putida was not allosterically regulated by a number of metabolites which may play an important role in the catabolism of D-fructose.

scholarly journals Guanine deaminase in rat liver and mouse liver and brain

1972 ◽  
Vol 128 (5) ◽  
pp. 1079-1088 ◽  
Author(s):  
K. S Kumar ◽  
A. Sitaramayya ◽  
P. S. Krishnan
Keyword(s):  
Rat Brain ◽  
Rat Liver ◽  
Inhibitory Activity ◽  
Substrate Concentration ◽  
Mouse Liver ◽  
Deae Cellulose ◽  
The Other ◽  
Guanine Deaminase ◽  
Sigmoidal Kinetics ◽  
Km Value

1. The guanine deaminase in rat liver supernatant preparations was resolved into two fractions, A and B, on DEAE-cellulose columns. The two differed in electrophoretic mobility and in various properties. The most noteworthy distinction between A and B components was that the enzyme A activity showed a sigmoid dependence on substrate concentration whereas the enzyme B showed classical Michaelis–Menten kinetics. The Km value of enzyme A for guanine was 5.3μm and that of enzyme B 20μm. 2. The entire guanine deaminase activity of mouse liver was contained in the 15000g supernatant of iso-osmotic homogenates. 3. A reinvestigation of the behaviour of rat brain 15000g supernatant guanine deaminase isoenzymes revealed that one enzyme had sigmoidal kinetics and the other enzyme showed a hyperbolic response. 4. Of the guanine deaminase in mouse brain iso-osmotic sucrose homogenate 80% was recovered in the 15000g supernatant and the rest from the particles. The supernatant guanine deaminase was resolvable into two fractions on DEAE-cellulose columns. One enzyme showed sigmoidal kinetics whereas the other showed a hyperbolic response to increasing substrate concentration; the Km values for the reaction with guanine were respectively 5 and 66μm. 5. The particulate fractions of mouse liver and brain were devoid of any overt inhibitory activity.

Understanding the risks and rewards of using 50% vs. 10% strength peroxide in pulp bleach plants

TAPPI Journal ◽  
2018 ◽  
Vol 17 (11) ◽  
pp. 601-607
Author(s):  
Alan Rudie ◽  
Peter Hart
Keyword(s):  
Hydrogen Peroxide ◽  
Reaction Rate ◽  
The Other ◽  
Mechanical Pulp ◽  
Engineering Controls ◽  
Point Of Use ◽  
Process Failure

The use of 50% concentration and 10% concentration hydrogen peroxide were evaluated for chemical and mechanical pulp bleach plants at storage and at point of use. Several dangerous occurrences have been documented when the supply of 50% peroxide going into the pulping process was not stopped during a process failure. Startup conditions and leaking block valves during maintenance outages have also contributed to explosions. Although hazardous events have occurred, 50% peroxide can be stored safely with proper precautions and engineering controls. For point of use in a chemical bleach plant, it is recommended to dilute the peroxide to 10% prior to application, because risk does not outweigh the benefit. For point of use in a mechanical bleach plant, it is recommended to use 50% peroxide going into a bleach liquor mixing system that includes the other chemicals used to maintain the brightening reaction rate. When 50% peroxide is used, it is critical that proper engineering controls are used to mitigate any risks.

Biodegradation of chlorophenols by immobilized pure-culture microorganisms

1996 ◽  
Vol 34 (10) ◽  
pp. 67-72 ◽  
Author(s):  
Lu Chih-Jen ◽  
Lee Chi-Mei ◽  
Huang Chiou-Zong
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Pseudomonas Putida ◽  
Pure Culture ◽  
The Other ◽  
Batch Reactors ◽  
Agrobacterium Radiobacter ◽  
Culture Cells ◽  
Lag Period

The biodegradation of phenol and chlorophenols by immobilized pure-culture cells was conducted by a series of batch reactors. The microorganisms used in this study were Pseudomonas putida, Psuedomonas testosteroni, Pseudomonas aeruginosa, and Agrobacterium radiobacter. All four species showed the ortho-cleavage pathway to metabolize chlorophenols. Among the four species, P. testosteroni, P. putida, and P. aeruginosa could effectively remove phenol at 200 mg/l. P. testosteroni could effectively remove 2-chlorophenol at 10mg/l. However, the other three species, P. putida, P. aeruginosa, and A. radiobacter, could not effectively remove 2-chlorophenol. Although 3-chlorophenol is a recalcitrant compound, P. testosteroni also could rapidly metabolize 3-chlorophenol at 10 mg/l. The removal of 4-chlorophenol at 10 mg/l by P. testosteroni reached 98% within one day. P. aeruginosa and A. radiobacter also could metabolize 4-chlorophenol after 2 and 7 days of lag period, respectively.

scholarly journals Differential biochemical and kinetic properties of α-amylases from Rhyzopertha dominica (F.) progenies reared on wheat varieties differing in α-amylase inhibitory activity

2021 ◽  
Vol 90 ◽  
pp. 101748
Author(s):  
Carlos R. González-Ruiz ◽  
Carmen L. Del Toro-Sánchez ◽  
Yaeel I. Cornejo-Ramírez ◽  
Francisco Rodríguez-Félix ◽  
Francisco J. Wong-Corral ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Rhyzopertha Dominica ◽  
Kinetic Properties ◽  
Wheat Varieties

Selective sensing of adenosine monophosphate (AMP) over adenosine diphosphate (ADP), adenosine triphosphate (ATP), and inorganic phosphates with zinc(II)-dipicolylamine-containing gold nanoparticles

2021 ◽  
Author(s):  
Lena Reinke ◽  
Marcus Koch ◽  
Christine Müller-Renno ◽  
Stefan Kubik
Keyword(s):  
Gold Nanoparticles ◽  
Adenosine Triphosphate ◽  
Triethylene Glycol ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate ◽  
Mixed Monolayer ◽  
Inorganic Phosphates

Mixed monolayer-protected gold nanoparticles containing surface-bound triethylene glycol and dipicolylamine groups aggregated in water/methanol, 1:2 (v/v) in the presence of nucleotides, if the solution also contained zinc(II) nitrate to convert...

scholarly journals ON THE LOCALIZATION OF SOME PHOSPHATASES IN THREE DIFFERENT SEGMENTS OF THE PROXIMAL TUBULES IN THE RAT KIDNEY

1967 ◽  
Vol 15 (8) ◽  
pp. 456-469 ◽  
Author(s):  
N. O. JACOBSEN ◽  
F. JØRGENSEN ◽  
Å. C. THOMSEN
Keyword(s):  
Adenosine Triphosphate ◽  
Rat Kidney ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate ◽  
Proximal Tubules ◽  
Reaction Pattern ◽  
Cytoplasmic Bodies ◽  
Acid And Alkaline Phosphatase ◽  
Convoluted Tubules

The distribution of several phosphatases in three segments of the proximal tubules was studied in frozen sections of glutaraldehyde-fixed rat kidneys. Two segments of the convoluted tubules were identified by in vivo injection of trypan blue. By increasing the concentration of adenosine triphosphate to 3 mM in the Wachstein and Meisel ATPase medium, a clear segmental differentiation in the reaction pattern of the brush border, cytoplasmic bodies and basal infoldings of the proximal tubules was obtained. The specificity of the reaction was investigated by substituting adenosine diphosphate, adenosine monophosphate or β-glycerophosphate for adenosine triphosphate in the incubation medium and by employing cyanide or fluoride as inhibitors. The reaction pattern was also compared with the localization of acid and alkaline phosphatase activities. In addition, the distribution of glucose 6-phosphatase activity was studied which showed differences in the three segments of the proximal tubules.

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