Quantitative relationships between structure and dissociation constants of enzyme - substrate complexes of microsomal cytochrome p-450 with derivatives of urea, diphenyl, diphenylmethane, and carbamide-containing heterocycles

1999 ◽  
Vol 33 (12) ◽  
pp. 644-650 ◽  
Author(s):  
A. I. Khlebnikov ◽  
R. R. Akhmedzhanov ◽  
O. I. Naboka ◽  
T. P. Novozheeva ◽  
A. S. Saratikov
Keyword(s):  
Dissociation Constants ◽  
Microsomal Cytochrome ◽  
Enzyme Substrate ◽  
Cytochrome P 450 ◽  
Derivatives Of

The role of secondary alcoholic groups of D-galacturonan in its degradation with exo-D-galacturonanase

1980 ◽  
Vol 45 (2) ◽  
pp. 427-434 ◽  
Author(s):  
Kveta Heinrichová ◽  
Rudolf Kohn
Keyword(s):  
Acetyl Derivative ◽  
Competitive Inhibitor ◽  
Hydroxyl Groups ◽  
Pectic Acid ◽  
Substrate Complex ◽  
Enzyme Substrate ◽  
The Individual ◽  
Degradation Degree ◽  
Derivatives Of

The effect of exo-D-galacturonanase from carrot on O-acetyl derivatives of pectic acid of variousacetylation degree was studied. Substitution of hydroxyl groups at C(2) and C(3) of D-galactopyranuronic acid units influences the initial rate of degradation, degree of degradation and its maximum rate, the differences being found also in the time of limit degradations of the individual O-acetyl derivatives. Value of the apparent Michaelis constant increases with increase of substitution and value of Vmax changes. O-Acetyl derivatives act as a competitive inhibitor of degradation of D-galacturonan. The extent of the inhibition effect depends on the degree of substitution. The only product of enzymic reaction is D-galactopyranuronic acid, what indicates that no degradation of the terminal substituted unit of O-acetyl derivative of pectic acid takes place. Substitution of hydroxyl groups influences the affinity of the enzyme towards the modified substrate. The results let us presume that hydroxyl groups at C(2) and C(3) of galacturonic unit of pectic acid are essential for formation of the enzyme-substrate complex.

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