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. 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 1.

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

Enzyme kcat (s-1) Km (μM) Metal content (eq)
FL-L1 w/ Mna 13 ± 1 5 ± 1 0.3Mn/0.4Fe/0.6Zn(II)
FL-L1 w/ Zn(II)a 28 ± 2 6 ± 1 0.1Fe/1.9Zn(II)
FL-L1 w/ Fea 3.6 ± 0.1 6 ± 1 0.9Fe/0.3Zn(II)
FL-L1 in LB mediumb 26 ± 1 4 ± 1 1.9 ± 0.1 Zn(II)
FL-L1 in minimal mediumb 10 ±1 4 ± 1 0.4Fe/0.3Zn(II)
a

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

b

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