scholarly journals The nature of the transition state for enzyme-catalyzed phosphoryl transfer. Hydrolysis of O-aryl phosphorothioates by alkaline phosphatase

Biochemistry ◽  
1995 ◽  
Vol 34 (38) ◽  
pp. 12255-12264 ◽  
Author(s):  
Florian Hollfelder ◽  
Daniel Herschlag
Keyword(s):  
Alkaline Phosphatase ◽  
Transition State ◽  
Phosphoryl Transfer ◽  
Hydrolysis Of

Extracellular enzymatic activities in the aquatic ecosystems of the Danube Delta. 2. Alkaline phosphatase activity

2021 ◽  
Vol 26 (1) ◽  
pp. 2269-2274
Author(s):  
IOAN PĂCEŞILĂ ◽  
EMILIA RADU
Keyword(s):  
Alkaline Phosphatase ◽  
Water Column ◽  
Aquatic Ecosystems ◽  
Temporal Dynamics ◽  
Extracellular Enzyme ◽  
Danube Delta ◽  
Phytoplankton Communities ◽  
Extracellular Enzymatic Activities ◽  
Adjacent Channels ◽  
Hydrolysis Of

Phosphorus is one of the most important inorganic nutrients in aquatic ecosystems, the development and functioning of the phytoplankton communities being often correlated with the degree of availability in assimilable forms of this element. Alkaline phosphatase (AP) is an extracellular enzyme with nonspecific activity that catalyses the hydrolysis of a large variety of organic phosphate esters and release orthophosphates. During 2011-2013, AP Activity (APA) was assessed in the water column and sediments of several aquatic ecosystems from Danube Delta: Roșu Lake, Mândra Lake and their adjacent channels – Roșu-Împuțita and Roșu-Puiu. The intensity of APA widely fluctuated, ranging between 230-2578 nmol p-nitrophenol L-1h-1 in the water column and 2104-15631 nmol p-nitrophenol g-1h-1 in sediment. Along the entire period of the study, APA was the most intense in Roșu-Împuțita channel, for both water and sediment samples. Temporal dynamics revealed its highest values in summer for the water column and in autumn for sediment. Statistical analysis showed significant seasonal diferences of the APA dynamics in spring vs. summer and autumn for the water column, and any relevant diferences for sediment.

scholarly journals Chicken Intestinal Alkaline Phosphatase

1960 ◽  
Vol 43 (6) ◽  
pp. 1149-1169 ◽  
Author(s):  
M. Kunitz
Keyword(s):  
Alkaline Phosphatase ◽  
Zinc Ions ◽  
Magnesium Ions ◽  
Intestinal Alkaline Phosphatase ◽  
Reversible Inactivation ◽  
Higher Temperature ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Zn Ions ◽  
Denaturation Of Proteins

Purified chicken intestinal alkaline phosphatase is active at pH 8 to 9, but becomes rapidly inactivated with change of pH to 6 or less. Also, a solution of the inactivated enzyme at pH 4.5 rapidly regains its activity at pH 8. In the range of pH 6 to 8 a solution of purified alkaline phosphatase consists of a mixture of active and inactive enzyme in equilibrium with each other. The rate of inactivation at lower pH and of reactivation at higher pH increases with increase in temperature. Also, the activity at equilibrium in the range of pH 6 to 8 increases with temperature so that a solution equilibrated at higher temperature loses part of its activity on cooling, and vice versa, a rise in temperature shifts the equilibrium toward higher activity. The kinetics of inactivation of the enzyme at lower pH and the reactivation at higher pH is that of a unimolecular reaction. The thermodynamic values for the heat and entropy of the reversible inactivation and reactivation of the enzyme are considerably lower than those observed for the reversible denaturation of proteins. The inactivated enzyme at pH 4 to 6 is rapidly reactivated on addition of Zn ions even at pH 4 to 6. However, zinc ions are unable to replace magnesium ions as cocatalysts for the enzymatic hydrolysis of organic phosphates by alkaline phosphatase.

scholarly journals Phosphatase synthesis in Klebsiella (Aerobacter) aerogenes growing in continuous culture

1972 ◽  
Vol 127 (1) ◽  
pp. 87-96 ◽  
Author(s):  
P. G. Bolton ◽  
A. C. R. Dean
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Continuous Culture ◽  
Activity Profile ◽  
Glucose Effect ◽  
Ph Values ◽  
Nitrophenyl Phosphate ◽  
Wide Range ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of

1. Phosphatase synthesis was studied in Klebsiella aerogenes grown in a wide range of continuous-culture systems. 2. Maximum acid phosphatase synthesis was associated with nutrient-limited, particularly carbohydrate-limited, growth at a relatively low rate, glucose-limited cells exhibiting the highest activity. Compared with glucose as the carbon-limiting growth material, other sugars not only altered the activity but also changed the pH–activity profile of the enzyme(s). 3. The affinity of the acid phosphatase in glucose-limited cells towards p-nitrophenyl phosphate (Km 0.25–0.43mm) was similar to that of staphylococcal acid phosphatase but was ten times greater than that of the Escherichia coli enzyme. 4. PO43−-limitation derepressed alkaline phosphatase synthesis but the amounts of activity were largely independent of the carbon source used for growth. 5. The enzymes were further differentiated by the effect of adding inhibitors (F−, PO43−) and sugars to the reaction mixture during the assays. In particular, it was shown that adding glucose, but not other sugars, stimulated the rate of hydrolysis of p-nitrophenyl phosphate by the acid phosphatase in carbohydrate-limited cells at low pH values (<4.6) but inhibited it at high pH values (>4.6). Alkaline phosphatase activity was unaffected. 6. The function of phosphatases in general is discussed and possible mechanisms for the glucose effect are outlined.

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