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Literature summary for 3.13.2.1 extracted from

  • Li, Q.S.; Cai, S.; Borchardt, R.T.; Fang, J.; Kuczera, K.; Middaugh, C.R.; Schowen, R.L.
    Comparative kinetics of cofactor association and dissociation for the human and trypanosomal S-adenosylhomocysteine hydrolases. 1. Basic features of the association and dissociation processes (2007), Biochemistry, 46, 5798-5809.
    View publication on PubMed
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Application

Application Comment Organism
medicine the cofactor NAD+ always dissociates more rapidly from Trypanosoma cruzi enzyme than from human enzyme, and binds more rapidly to human than to trypanosomal enzyme Homo sapiens
medicine the cofactor NAD+ always dissociates more rapidly from Trypanosoma cruzi enzyme than from human enzyme, and binds more rapidly to human than to trypanosomal enzyme Trypanosoma cruzi

Inhibitors

Inhibitors Comment Organism Structure
beta-thionicotinamide adenine dinucleotide binding affinity 40 nM, 30% loss of activity after 12 h Homo sapiens
beta-thionicotinamide adenine dinucleotide binding affinity 0.0006-0.015 mM, 60% loss of activity after 30 min Trypanosoma cruzi
beta-thionicotinamide adenine dinucleotide, reduced form binding affinity 40 nM, 30% loss of activity after 12 h Homo sapiens
beta-thionicotinamide adenine dinucleotide, reduced form binding affinity 0.0006-0.015 mM, 100% loss of activity after 30 min Trypanosoma cruzi

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Trypanosoma cruzi
-
-
-

Cofactor

Cofactor Comment Organism Structure
NAD+ enzyme exhibits two classes of active sites, one binding NAD+ weakly and generating full activity very rapidly, the other binding the cofactor more strongly but generating activity only slowly. Final affinity of enzyme for NAD+ is about micromolar. Slow binding exhibits saturation kinetics with a rate constant of 0.006 per s. Dissociation of NAD+ from all binding sites is a single first-order reaction. The cofactor always dissociates more rapidly from Trypanosoma cruzi enzyme than from human enzyme, and binds more rapidly to human than to trypanosomal enzyme Trypanosoma cruzi
NAD+ enzyme exhibits two classes of active sites, one binding NAD+ weakly and generating full activity very rapidly, the other binding the cofactor more strongly but generating activity only slowly. Slow binding exhibits saturation kinetics with a rate constant of 0.06 per s. Dissociation of NAD+ from all binding sites is a single first-order reaction. The cofactor always dissociates more rapidly from Trypanosoma cruzi enzyme than from human enzyme, and binds more rapidly to human than to trypanosomal enzyme Homo sapiens