. Author manuscript; available in PMC: 2009 Oct 20.

Published in final edited form as: Biochemistry. 2005 Dec 27;44(51):16866–16874. doi: 10.1021/bi051898d

Table 4.

Stability of the E·S complex formed with mutant or wild type MSOX and L-proline

	dissociation constant (mM)
	kinetically determined			spectral titration

	K_d	PH	pK_a	K_d (mM)	pH
Tyr317Phe	90 ± 30^a	⋘ pK_a	9.0 ± 0.4^a
	109 ± 8	7.6		101 ± 4	7.6
	440 ± 25	9.6		420 ± 40	9.6
	510 ± 10^a	⋙ pK_a
wild type	256 ± 4^b	6.5 to 9.0	nd^c	200 ± 6	7.2
				230 ± 9	8.6

Values were determined based on the fit of data, obtained in the pH range from 7.5 to 10.0, to equation 4, as described in the text.

Average value previously reported by Zhao and Jorns (14) based on data obtained in the pH range from 6.5 to 9.0, including K_d values observed at pH 7.2 (241 ± 12 mM ) and pH 8.6 (248 ± 16 mM).

Not detected.