TABLE 1.

Enzyme activity of 20 to 50% saturated ammonium sulfate extracts of E. coli transformed with pYA1170b or with the blank cloning vector pET16b

Substrate	Activity (nmol min−1 mg of protein−1) (n = 3)
	Rv1170	Blank vector
MSmBa	1.2 ± 0.1	<0.002
MSmBb	<10−4	NDf
GlcNAc-Insc	27 ± 2	<0.002
GlcNAcc	0.087 ± 0.005	<0.005
MSHd	0.002 ± 0.001	ND
MSHe	<10−4	ND

^aAnalysis for AcCySmB produced by amidase cleavage. 

^bAnalysis for production of the deacetylase product CySmB-GlcN-Ins. 

^cAnalysis for corresponding amine resulting from deacetylase reaction. 

^dAnalysis for AcCys produced by amidase cleavage. 

^eAnalysis for production of the deacetylase product Cys-GlcN-Ins. 

^fND, not determined.