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Literature summary extracted from

  • Nishina, Y.; Sato, K.; Tamaoki, H.; Tanaka, T.; Setoyama, C.; Miura, R.; Shiga, K.
    Molecular mechanism of the drop in the pKa of a substrate analog bound to medium-chain acyl-CoA dehydrogenase: implications for substrate activation (2003), J. Biochem., 134, 835-842.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
1.3.8.7 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.8.7 kidney
-
Sus scrofa
-

Synonyms

EC Number Synonyms Comment Organism
1.3.8.7 MCAD
-
Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.8.7 7,8-dichloro-FAD artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand Sus scrofa
1.3.8.7 8-amino-FAD artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand Sus scrofa
1.3.8.7 8-chloro-FAD artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand Sus scrofa
1.3.8.7 8-cyano-FAD artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand Sus scrofa
1.3.8.7 8-methoxy-FAD artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand Sus scrofa
1.3.8.7 ribityl-2'-deoxy-8-chloro-FAD artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand Sus scrofa
1.3.8.7 ribityl-2'-deoxy-8-cyano-FAD artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand Sus scrofa