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Literature summary 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

Application

EC Number Application Comment Organism
3.13.2.1 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
3.13.2.1 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

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

Organism

EC Number Organism UniProt Comment Textmining
3.13.2.1 Homo sapiens
-
-
-
3.13.2.1 Trypanosoma cruzi
-
-
-

Cofactor

EC Number Cofactor Comment Organism Structure
3.13.2.1 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
3.13.2.1 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