Involvement of histidine residues in catalytic activity of xanthine dehydrogenase from hen liver.
1. Modification of histidine residue(s) of xanthine dehydrogenase from hen liver by DEP and photooxidation results in loss of the ability to transfer electrons from xanthine to NAD+ and also from NADH to 2,6-dichlorophenolindophenol (DCIP). 2. The kinetics of inactivation suggest that carbethoxylation of more than one histidyl residue in the enzyme may be responsible for the inactivation.
Zakrzewska
B
B
Department of Comparative Biochemistry, Polish Academy of Sciences, Warsaw.
Kamiński
Z W
ZW
D015086:2,6-Dichloroindophenol / Q000378:metabolism; D000818:Animals; D002645:Chickens; D004047:Diethyl Pyrocarbonate / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D005260:Female; D006639:Histidine / Q000737:chemistry*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D009243:NAD / Q000378:metabolism; D010084:Oxidation-Reduction; D010777:Photochemistry; D013329:Structure-Activity Relationship; D019820:Xanthine; D014968:Xanthine Dehydrogenase / Q000737:chemistry / Q000378:metabolism*; D014970:Xanthines / Q000378:metabolism
D014970:Xanthines; D009243:NAD; D019820:Xanthine; D006639:Histidine; D015086:2,6-Dichloroindophenol; D014968:Xanthine Dehydrogenase; D004047:Diethyl Pyrocarbonate