BADH-NAD+-K+ Complex Interaction Studies Reveal a New Possible Mechanism between Potassium and Glutamic 254 at the Coenzyme Binding Site

2022 ◽  
Author(s):  
César Muñoz-Bacasehua ◽  
Hisila Santacruz-Ortega ◽  
Elisa M. Valenzuela-Soto
Keyword(s):  
Binding Site ◽  
Complex Interaction ◽  
Coenzyme Binding ◽  
Interaction Studies ◽  
Coenzyme Binding Site

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.

scholarly journals Affinity labelling of the NADP+-binding site of glucose 6-phosphate dehydrogenase from Candida utilis

1979 ◽  
Vol 183 (2) ◽  
pp. 297-302 ◽  
Author(s):  
T Bellini ◽  
M Signorini ◽  
F Dallocchio ◽  
M Rippa
Keyword(s):  
Binding Site ◽  
Candida Utilis ◽  
Aldehyde Group ◽  
Lysine Residue ◽  
Reversible Inactivation ◽  
Coenzyme Binding ◽  
Complete Inactivation ◽  
Affinity Labelling ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Coenzyme Binding Site

1. Periodate-oxidized NADP+ inhibits the catalytic activity of glucose 6-phosphate dehydrogenase from Candida utilis, competing with NADP+. 2. Incubation of the enzyme with the coenzyme analogue causes partial reversible inactivation of the enzyme as a result of affinity labelling of the coenzyme-binding site. 3. Some kinetic values of the reaction were calculated. 4. The inactivation can be made irreversible by treatment with NaBH4, which reduces a Schiff base formed between an aldehyde group on the coenzyme analogue and a lysine residue on the enzyme. 5. Complete inactivation can be correlated with the binding of only one inhibitor to each enzyme subunit. 6. The lysine residue involved in the binding of the inhibitor is present at the coenzyme-binding site.

Sign in / Sign up

Export Citation Format

Share Document