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

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

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.

scholarly journals Study of Coenzyme Binding Site of Octopine Dehydrogenase Using Analogues of NAD+

1975 ◽  
Vol 56 (1) ◽  
pp. 109-116 ◽  
Author(s):  
Anna OLOMUCKI ◽  
Francoise THOME-BEAU ◽  
Jean-Francois BIELLMANN ◽  
Guy BRANLANT
Keyword(s):  
Binding Site ◽  
Coenzyme Binding ◽  
Octopine Dehydrogenase ◽  
Coenzyme Binding Site

scholarly journals Evidence for an arginine residue at the coenzyme-binding site of Escherichia coli isocitrate dehydrogenase

1989 ◽  
Vol 261 (1) ◽  
pp. 301-304 ◽  
Author(s):  
J S McKee ◽  
H G Nimmo
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Isocitrate Dehydrogenase ◽  
Arginine Residue ◽  
Order Process ◽  
First Order ◽  
Coenzyme Binding ◽  
Phosphorylated Form ◽  
Specific Reagent ◽  
Coenzyme Binding Site

The arginine-specific reagent phenylglyoxal inactivated the active, dephosphorylated, form of Escherichia coli isocitrate dehydrogenase rapidly in a pseudo-first-order process. Both NADP+ and NADPH protected the enzyme against inactivation. Phenylglyoxal appeared to react with one arginine residue per subunit, and the extent of the reaction was proportional to the extent of the inactivation. In contrast, the phosphorylated form of isocitrate dehydrogenase did not react detectably with phenylglyoxal. The data indicate that the coenzyme-binding site of isocitrate dehydrogenase contains a reactive arginine residue that is protected by phosphorylation, and are consistent with the hypothesis that phosphorylation of the enzyme occurs close to or at its active site.

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