Glyceryl-ether monooxygenase (EC 1.14.16.5): nature of the glyceryl-ether lipid substrates in aqueous buffer.
The kinetics of inhibition of glyceryl-ether monooxygenase with 6-methyl-5,6,7,8-tetrahydropterin as cofactor (saturating) by the detergent Mega-10 with batyl alcohol and (RS)-3-(1-hexadecyloxy)-2-hydroxypropane-1-phosphocholine as substrates exhibited noncompetitive inhibition with apparent Ki values of 1.74 +/- 0.37 mM and 185 +/- 23 microM, respectively. Inhibition by octadecan-1-ol (with batyl alcohol as substrate in the presence of 2.3 mM Mega-10) was competitive with an apparent Ki value of 765 +/- 80 microM. The critical micelle concentration values of various solutions of Mega-10 were determined and used to show that the active ether-lipid substrates were in micelle form (for a water soluble substrate) or mixed micelle form (for substrates solubilised with Mega-10).
Taguchi
H
H
Department of Natural Science, Kyoto Women's University, Japan.
Kosar-Hashemi
B
B
Paal
B
B
Yang
N
N
Armarego
W L
WL
D000818:Animals; D002021:Buffers; D003902:Detergents / Q000494:pharmacology; D005227:Fatty Acids / Q000494:pharmacology*; D005233:Fatty Alcohols / Q000494:pharmacology; D005944:Glucosamine / Q000031:analogs & derivatives* / Q000494:pharmacology; D005995:Glyceryl Ethers / Q000378:metabolism*; D007700:Kinetics; D008823:Micelles; D008854:Microscopy, Electron; D008862:Microsomes, Liver / Q000201:enzymology* / Q000648:ultrastructure; D006899:Mixed Function Oxygenases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011622:Pterins / Q000378:metabolism; D051381:Rats; D012995:Solubility; D013379:Substrate Specificity
D002021:Buffers; D003902:Detergents; D005227:Fatty Acids; D005233:Fatty Alcohols; D005995:Glyceryl Ethers; D008823:Micelles; D011622:Pterins; C009316:stearyl alcohol; C033433:batyl alcohol; C042221:decanoyl-N-methylglucamide; C017523:6-methyltetrahydropterin; D006899:Mixed Function Oxygenases; C020678:glyceryl-ether monooxygenase; D005944:Glucosamine