. Author manuscript; available in PMC: 2009 Sep 24.

Published in final edited form as: Biochemistry. 2008 Jul 3;47(30):7947–7953. doi: 10.1021/bi8004768

Table 2.

Steady-state kinetic and metal content data for L1 folded in the cytoplasm (M-L1). Substrate used in the kinetic studies was nitrocefin, and kinetic studies were conducted as described in Materials and Methods

Enzyme	k_cat (s^-1)	K_m (μM)	Metal content (eq)
M-L1 w/ Mn(II)^a	4.2 ± 0.4	2.1 ± 0.9	0.4 Mn; 0.4Zn; 0.4 Fe
M-L1 w/ Zn(II)^a	21 ± 1	7.0 ± 1.1	0.3 Fe ; 1.2 Zn(II)
M-L1 w/ Fe(II)^a	<0.1	N/A	1.5 Fe; 0.1 Zn(II)
M-L1 in minimal medium^b	<0.1	N/A	0.2 Mn;0.7 Fe;0.1 Zn(II)
M-L1 in LB medium^b	10 ± 1	1.0 ± 0.2	0.7 Fe; 0.6 Zn(II)

L1 was over-expressed in minimal medium containing 50 μM of the indicated metal ion as described in Materials and Methods.

L1 was over-expressed in minimal or LB medium without adding any additional metal ions.