Table 2.

Dissociation constants of human AZ_95–228-ODC heterodimers.

AZ95–228-ODC dimer	1Kd,AZ-ODC (μM)	2 Fold Change (Kd,mutant/Kd,WT)
AZ95–228-ODC	1.15 ± 0.01	1
AZ95–228_E142A-ODC	2.20 ± 0.02	1.9
AZ95–228_K153A-ODC	1.21 ± 0.01	1.05
AZ95–228_D154A-ODC	1.70 ± 0.02	1.5
AZ95–228_E161A-ODC	1.11 ± 0.01	0.97
AZ95–228_E164A-ODC	1.68 ± 0.01	1.46
AZ95–228_E165A-ODC	1.73 ± 0.02	1.5
AZ95–228_H171A-ODC	2.03 ± 0.02	1.77
AZ95–228_K178A-ODC	3.03 ± 0.02	2.63
AZ95–228-3Mα1-ODC	6.58 ± 0.02	5.72
AZ95–228-3Mα1_D154A	3.39 ± 0.03	2.95
AZ95–228-3Mα1_E161A-ODC	4.97 ± 0.06	4.32
AZ95–228-5Mα1-ODC	6.81 ± 0.06	5.92
AZ95–228-3Mα1_E142A-ODC	8.86 ± 0.05	7.7
AZ95–228-3Mα1_H171A-ODC	8.55 ± 0.08	7.43
AZ95–228-3Mα1_K178A-ODC	7.67 ± 0.06	6.67
AZ95–228_E142A/H171A/K178A-ODC	11.49 ± 0.6	10
AZ95–228-8M-ODC	12.44 ± 0.7	10.8

¹ The dissociation constants (K_d) of AZ_95–228-ODC dimer were derived by globally fitting the sedimentation velocity data (Figure 3 and Figure S3) to the A + B↔AB hetero-association model in the SEDPHAT program [50]. ² Fold change was the ratio of K_d,AZ-ODC of the mutant versus K_d,AZ-ODC of WT.