Microsomal Hydroxylation and Glucuronidation of [6]-Gingerol

2006 ◽  
Vol 54 (23) ◽  
pp. 8769-8774 ◽  
Author(s):  
Erika Pfeiffer ◽  
Franziska F. Heuschmid ◽  
Stefan Kranz ◽  
Manfred Metzler
Keyword(s):  
Microsomal Hydroxylation

Absence of isotope effects in the microsomal hydroxylation of acetanilide

1967 ◽  
Vol 16 (11) ◽  
pp. 2230-2233 ◽  
Author(s):  
Tanabe Masato ◽  
Dennis Yasuda ◽  
Josephine Tagg ◽  
Mitoma Chozo
Keyword(s):  
Isotope Effects ◽  
Microsomal Hydroxylation

scholarly journals Structural requirements for the utilization of ascorbate analogues in the prolyl 4-hydroxylase reaction

1994 ◽  
Vol 300 (1) ◽  
pp. 75-79 ◽  
Author(s):  
G Tschank ◽  
J Sanders ◽  
K H Baringhaus ◽  
F Dallacker ◽  
K I Kivirikko ◽  
...  
Keyword(s):  
Negative Charge ◽  
Substrate Inhibition ◽  
Side Chain ◽  
Structural Requirements ◽  
Response Behaviour ◽  
Structural Analogues ◽  
Microsomal Hydroxylation ◽  
Ring Position ◽  
Charged Group ◽  
Positively Charged

The ability of structural analogues of ascorbate to serve as substitutes for this reducing agent in the prolyl 4-hydroxylase reaction was studied. In experiments using the purified enzyme, variations of the compounds′ side chain were compatible with co-substrate activity. The presence of very large hydrophobic substituents or a positively charged group caused an increase in the observed Km values. A negative charge and smaller modifications did not change the affinity to the enzyme when compared with L-ascorbate. 6-Bromo-6-deoxy-L-ascorbate had a lower Km than the physiological reductant. Substitution at the -OH group in ring position 3 prevented binding to the enzyme. The same pattern of activity was observed when the full and uncoupled prolyl 4-hydroxylase reactions were studied. The Vmax. values with all compounds were similar. The reaction of microsomal prolyl 4-hydroxylase was supported by D-isoascorbate, O6-tosyl-L-ascorbate and 5-deoxy-L-ascorbate, giving the same dose-response behaviour as L-ascorbate itself. Again, 6-bromo-6-deoxy-L-ascorbate gave a lower Km and a similar Vmax. value. L-Ascorbic acid 6-carboxylate produced substrate inhibition at concentrations above 0.3 mM. The Km and Vmax. values calculated from concentrations up to 0.2 mM were similar to those of L-ascorbate. The enzyme activity observed with 6-amino-6-deoxy-L-ascorbate was very low in the microsomal hydroxylation system. The calculated Vmax. value was lower than that of L-ascorbate, suggesting a restriction of the access of this compound to the enzyme.

The Effects of the Non-ionic Detergent Tween 80 on Hepatic Microsomal Hydroxylation

Xenobiotica ◽  
1975 ◽  
Vol 5 (5) ◽  
pp. 261-277 ◽  
Author(s):  
M. Danny Burke ◽  
James W. Bridges ◽  
Dennis V. Parke
Keyword(s):  
Tween 80 ◽  
Ionic Detergent ◽  
Microsomal Hydroxylation
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