. Author manuscript; available in PMC: 2012 Apr 1.

Published in final edited form as: Arch Biochem Biophys. 2011 Jan 22;508(1):25–30. doi: 10.1016/j.abb.2011.01.012

Table 4. Enzymatic activity of CoCBS and wild type FeCBS.

The CBS activity was determined in two reactions. In the classical reaction, homocysteine and L-serine were used to generate cystathionine. In the alternative reaction, hydrogen sulfide was generated by condensing L-cysteine and β-mercaptoethanol. The extent of saturation of enzyme with the PLP was tested by running the activity assays in the presence or absence of 0.5 mM PLP. The reactions were performed in the presence or absence of CBS allosteric activator AdoMet in final concentration of 0.3 mM.

Activity assay	PLP	AdoMet	CoCBS	FeCBS
Classical L-cystathionine-generation (U/mg of protein)	−	−	75 ± 5	77 ± 9
	−	+	204 ± 13	217 ± 15
	+	−	95 ± 3	101 ± 4
	+	+	372 ± 19	404 ± 25

Alternative H₂S-generation (U/mg of protein)	−	−	91 ± 6	112 ± 10
	−	+	318 ± 21	329 ± 25
	+	−	124 ± 11	139 ± 6
	+	+	409 ± 24	341 ± 17