N-Tosyl-l-phenylalanine Chloromethyl Ketone, a Serine Protease Inhibitor, Identifies Glutamate 398 at the Coenzyme-Binding Site of Human Aldehyde Dehydrogenase. Evidence for a Second “Naked Anion” at the Active Site†

Biochemistry ◽  
1998 ◽  
Vol 37 (40) ◽  
pp. 14151-14156 ◽  
Author(s):  
Marek Dryjanski ◽  
Lynda L. Kosley ◽  
Regina Pietruszko
Keyword(s):  
Protease Inhibitor ◽  
Binding Site ◽  
Serine Protease ◽  
Aldehyde Dehydrogenase ◽  
Active Site ◽  
Serine Protease Inhibitor ◽  
Chloromethyl Ketone ◽  
Coenzyme Binding ◽  
Coenzyme Binding Site

A Serine Protease Inhibitor, N-α-Tosyl-l-lysine Chloromethyl Ketone, Prolongs Rat Hepatic Allograft Survival

2001 ◽  
Vol 96 (2) ◽  
pp. 296-303 ◽  
Author(s):  
Jia-Lin Zhang ◽  
Yasuo Yamaguchi ◽  
Katsutaka Mori ◽  
Kazutoshi Okabe ◽  
Hideki Hidaka ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Serine Protease ◽  
Serine Protease Inhibitor ◽  
Allograft Survival ◽  
Chloromethyl Ketone ◽  
Hepatic Allograft

Characterization of the coenzyme binding site of liver aldehyde dehydrogenase: differential reactivity of coenzyme analogs

Biochemistry ◽  
1985 ◽  
Vol 24 (21) ◽  
pp. 5847-5851 ◽  
Author(s):  
Hedvig Von Bahr-Lindstroem ◽  
Reinhard Jeck ◽  
Christoph Woenckhaus ◽  
Sigrid Sohn ◽  
John Hempel ◽  
...  
Keyword(s):  
Binding Site ◽  
Aldehyde Dehydrogenase ◽  
Coenzyme Binding ◽  
Differential Reactivity ◽  
Liver Aldehyde Dehydrogenase ◽  
Coenzyme Binding Site

scholarly journals The action of chelating agents on human liver aldehyde dehydrogenase

1975 ◽  
Vol 151 (2) ◽  
pp. 443-445 ◽  
Author(s):  
R S Sidhu ◽  
A H Blair
Keyword(s):  
Binding Site ◽  
Aldehyde Dehydrogenase ◽  
Human Liver ◽  
Chelating Agents ◽  
Hydrophobic Interactions ◽  
Coenzyme Binding ◽  
Complexing Ability ◽  
Liver Aldehyde Dehydrogenase ◽  
Related Compounds ◽  
Coenzyme Binding Site

Human liver aldehyde dehydrogenase was inhibited by aromatic chelating agents. However, structurally related compounds with much lower metal-complexing ability displayed affinities for enzyme essentially equal to those of their respective chelating analogues. Inhibition was competitive with respect to the coenzyme. It is suggested that hydrophobic interactions between the inhibitors and the coenzyme-binding site of the enzyme are responsible for the observed effects on activity.

Characterization of a Structure Close to the Coenzyme-Binding Site of Liver Aldehyde Dehydrogenase

2005 ◽  
Vol 117 (3) ◽  
pp. 521-526 ◽  
Author(s):  
Hedvig BAHR-LINDSTRÖM ◽  
Hans JÖRNVALL ◽  
Sigrid SOHN ◽  
Christoph WOENCKHAUS ◽  
Reinhard JECK
Keyword(s):  
Binding Site ◽  
Aldehyde Dehydrogenase ◽  
Coenzyme Binding ◽  
Liver Aldehyde Dehydrogenase ◽  
Coenzyme Binding Site
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