scholarly journals Atropselective Hydrolysis of Chiral Binol-Phosphate Esters Catalyzed by the Phosphotriesterase from Sphingobium sp. TCM1

Biochemistry ◽  
2020 ◽  
Vol 59 (46) ◽  
pp. 4463-4469
Author(s):  
Dao Feng Xiang ◽  
Tamari Narindoshvili ◽  
Frank M. Raushel
Keyword(s):  
Phosphate Esters ◽  
Hydrolysis Of

Kinetics of the Hydrolysis of Phosphate Esters

1977 ◽  
Vol 46 (9) ◽  
pp. 828-841 ◽  
Author(s):  
Vladimir E Bel'skii
Keyword(s):  
Phosphate Esters ◽  
Kinetics Of ◽  
Hydrolysis Of

scholarly journals A Comparison of Human Leukocyte Phosphatase Activity toward Sodium β-Glycerophosphate, Adenosine 5'-Phosphate and Glucose 1-Phosphate

Blood ◽  
1959 ◽  
Vol 14 (4) ◽  
pp. 415-422 ◽  
Author(s):  
JAMES H. FOLLETTE ◽  
WILLIAM N. VALENTINE ◽  
JOHN REYNOLDS
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Cell Population ◽  
Alkaline Phosphatase Activity ◽  
Human Leukocyte ◽  
Maximal Activity ◽  
Phosphate Esters ◽  
Chronic Myelocytic Leukemia ◽  
Myelocytic Leukemia ◽  
Hydrolysis Of

Abstract The ability of human leukocyte enzymes to hydrolyze phosphorus is compared in terms of the conventional substrate sodium β-glycerophosphate and the metabolically important phosphate esters, adenosine 5'-phosphate and glucose 1-phosphate. At pH 9.9, there is marked and comparable variation in phosphatase activity toward all three substrates, this being low in chronic myelocytic leukemia and high in the presence of infection and certain "stressful" states. Moreover, substrate mixture experiments show no increased hydrolysis of phosphorus when two substrates are present in the incubation mixture. Increased phosphatase activity toward both glucose 1-phosphate and sodium β-glycerophosphate resulted when corticosteroids were administered in large doses for 72 hours. The data, while not providing absolute proof, are compatible with the hydrolysis of phosphorus at pH 9.9, being due in the case of all three substrates to the activity of the same phosphomonoesterase or group of phosphomonesterases. At pH 5.5, phosphatase activity toward both sodium β-glycerophosphate and adenosine 5'-phosphate was likewise demonstrated, but, in leukocytes, the pH of maximal activity varies from subject to subject and is dependent to a large extent on the amount of the highly variable "alkaline phosphatase" activity present in any given cell population at the time of analysis.

CATALYTIC HYDROLYSIS OF PHOSPHATE ESTERS IN MICROEMULSIONS. V. THE EFFECT OF COSURFACTANTS

1988 ◽  
Vol 9 (5) ◽  
pp. 493-510 ◽  
Author(s):  
Raymond A. Mackay ◽  
Beth A. Burnside ◽  
Stephanie M. Garlick ◽  
Barry L. Knier ◽  
H. Dupont Durst ◽  
...  
Keyword(s):  
Phosphate Esters ◽  
Catalytic Hydrolysis ◽  
Hydrolysis Of

Catalytic hydrolysis of phosphate esters in microemulsions

1988 ◽  
Vol 17 (1) ◽  
pp. 77-81 ◽  
Author(s):  
Barry L. Knier ◽  
H. Dupont Durst ◽  
Beth A. Burnside ◽  
Raymond A. Mackay ◽  
Frederick R. Longo
Keyword(s):  
Phosphate Esters ◽  
Catalytic Hydrolysis ◽  
Hydrolysis Of

Charge density distribution and theoretical analysis of low and high energy phosphate esters

RSC Advances ◽  
2015 ◽  
Vol 5 (117) ◽  
pp. 96623-96638 ◽  
Author(s):  
Adrian Mermer ◽  
Tadeusz Lis ◽  
Przemysław Starynowicz
Keyword(s):  
Density Distribution ◽  
Charge Density ◽  
Lone Pair ◽  
High Energy ◽  
Phosphate Esters ◽  
High Energy Phosphate ◽  
Charge Density Distribution ◽  
Oxygen Lone Pair ◽  
Hydrolysis Of ◽  
Experimental Charge Density

There is a strict relation between the energy of hydrolysis of phosphate esters and the extent of interactions between the p ester oxygen lone pair and the antibonding orbitals of the rest of the molecule. Its impact on experimental charge density distribution is analyzed.

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