EC Number | Cloned (Comment) | Organism |
---|---|---|
3.13.2.1 | expression in Escherichia coli | Trypanosoma cruzi |
3.13.2.1 | expression in Escherichia coli | Homo sapiens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.13.2.1 | K431A | mutant loses its cofactor binding affinity but retains the wild type's tetrameric structure | Trypanosoma cruzi |
3.13.2.1 | additional information | comparison of human and trypanosomal cofactor NAD+/NADH binding site. Among the 38 residues in this region, only four are different between the two enzymes. The four non-identical residues make no major contribution to differential cofactor binding between human SAHH and trypanosomal SAHH. Four pairs of identical residues are shown by free energy simulations to differentiate cofactor binding between both enzymes | Trypanosoma cruzi |
3.13.2.1 | additional information | comparison of human and trypanosomal cofactor NAD+/NADH binding site. Among the 38 residues in this region, only four are different between the two enzymes. The four non-identical residues make no major contribution to differential cofactor binding between human SAHH and trypanosomal SAHH. Four pairs of identical residues are shown by free energy simulations to differentiate cofactor binding between both enzymes | Homo sapiens |
3.13.2.1 | Y430A | mutation alters the NAD+ association and dissociation kinetics, increasing the cofactor equilibrium dissociation constant from approximately 10 nM to about 800 nM | Homo sapiens |
3.13.2.1 | Y435A | mutation alters the NAD+ association and dissociation kinetics, Y435A increases the cofactor equilibrium dissociation constant from approximately 100 nM to about 1 mM | Trypanosoma cruzi |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.13.2.1 | Homo sapiens | P23526 | - |
- |
3.13.2.1 | Trypanosoma cruzi | - |
- |
- |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
3.13.2.1 | NAD+ | comparison of human and trypanosomal cofactor NAD+/NADH binding site. Among the 38 residues in this region, only four are different between the two enzymes. The four non-identical residues make no major contribution to differential cofactor binding between human SAHH and trypanosomal SAHH. Four pairs of identical residues are shown by free energy simulations to differentiate cofactor binding between both enzymes. Calculation of association kinetics of NAD+ with human and trypanosomal enzyme | Trypanosoma cruzi | |
3.13.2.1 | NAD+ | comparison of human and trypanosomal cofactor NAD+/NADH binding site. Among the 38 residues in this region, only four are different between the two enzymes. The four non-identical residues make no major contribution to differential cofactor binding between human SAHH and trypanosomal SAHH. Four pairs of identical residues are shown by free energy simulations to differentiate cofactor binding between both enzymes. Calculation of association kinetics of NAD+ with human and trypanosomal enzyme. Y430 in the C-terminal extension of human SAHH may slightly influence binding of NAD+ and NADH to apo-SAHH | Homo sapiens |