scholarly journals Kinetic studies of the activation of adenosine triphosphate-lombricine phosphotransferase by magnesium ions

1964 ◽  
Vol 90 (1) ◽  
pp. 177-181 ◽  
Author(s):  
TJ Gaffney ◽  
WJ O'Sullivan
Keyword(s):  
Adenosine Triphosphate ◽  
Kinetic Studies ◽  
Magnesium Ions

scholarly journals Hereditary Nonspherocytic Hemolysis With Erythrocyte Phosphofructokinase Deficiency

Blood ◽  
1972 ◽  
Vol 39 (3) ◽  
pp. 415-425 ◽  
Author(s):  
Larry Waterbury ◽  
Eugene P. Frenkel
Keyword(s):  
Enzyme Activity ◽  
Adenosine Triphosphate ◽  
Lactate Production ◽  
Kinetic Studies ◽  
Glycogen Storage ◽  
Muscle Disease ◽  
Phosphofructokinase Activity ◽  
Phosphofructokinase Deficiency

Abstract Hereditary nonspherocytic hemolysis associated with abnormal erythrocyte phosphofructokinase activity was demonstrated in a young man. Enzyme activity in the propositus, his mother, and maternal grandmother was approximately 60% of normal controls. There was markedly increased lability of enzyme activity on in vitro storage. Kinetic studies revealed increased sensitivity to adenosine triphosphate inhibition. Erythrocyte adenosine triphosphate levels were depressed. The absence of muscle disease and the presence of normal in vivo lactate production following ischemic exercise differentiated this kindred from those with Type VII glycogen storage disease.

Mechanisms of inhibition of adenine phosphoribosyltransferase by adenine nucleosides and nucleotides

1970 ◽  
Vol 48 (5) ◽  
pp. 573-579 ◽  
Author(s):  
J. Frank Henderson ◽  
R. E. A. Gadd ◽  
H. M. Palser ◽  
M. Hori
Keyword(s):  
Adenosine Triphosphate ◽  
Kinetic Studies ◽  
Adenosine Diphosphate ◽  
Free Enzyme ◽  
Adenine Phosphoribosyltransferase ◽  
Enzyme Form

Kinetic studies of the inhibition of adenine phosphoribosyltransferase by adenine 6′-deoxyallofuranoside and 2′-deoxyadenylate indicate that both compounds bind to free enzyme and to the enzyme–phosphoribosylpyrophosphate complex, although they bind with different relative affinities to each enzyme form. The sites to which these inhibitors bind appear to be different from those to which substrates and products bind. Kinetic and physical studies show that adenosine diphosphate and adenosine triphosphate also bind to several enzyme forms, and that their mechanisms of inhibition of this enzyme are complex.

FACTORS INVOLVED IN THE BACTERIAL DECARBOXYLATION OF SUCCINIC ACID

1961 ◽  
Vol 7 (6) ◽  
pp. 889-893
Author(s):  
A. A. Yousten ◽  
E. A. Delwiche
Keyword(s):  
Succinic Acid ◽  
Adenosine Triphosphate ◽  
Coenzyme A ◽  
Magnesium Ions

The succinic decarboxylase system of Veillonella alcalescens loses activity when aged at 2 °C for a few days. Evolution of CO2 by aged extracts of this organism was greatly stimulated by boiled cell-free extracts of Propionibacterium pentosaceum. These boiled extracts could not be replaced by coenzyme A (CoA), adenosine triphosphate (ATP), magnesium ions, biotin, or dimethylbenzimidazolylcobamide coenzyme (DBC).

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