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. Author manuscript; available in PMC: 2008 Aug 12.
Published in final edited form as: Biochemistry. 2006 Jul 25;45(29):8988–8999. doi: 10.1021/bi0606602

Table 2.

Steady-State Kinetic Parameters for the α—Keto Acid-Independent Hydrolysis of Acyl-CoA Analogs Catalyzed by M. tuberculosis IPMSa.

Without added MgCl2
With added MgCl2
Km (μM) kcat (s−1) kcat/Km (s−1 M−1) Km (μM) kcat (s−1) kcat/Km (s−1 M−1)
Acetyl-CoA 370 ± 40 (6 ± 0.3) × 10−2 150 ± 19 160 ± 29 (3 ± 0.2)× 10−2 170 ± 36
Propionyl-CoA 220 ± 40 (4 ± 0.3) × 10−2 190 ± 36 NDb ND -
Crotonyl-CoA 50 ± 3 (5 ± 0.2) × 10−2 940 ± 72 95 ± 15 (4 ± 0.2)× 10−2 400 ± 70
a

. Performed at 25°C and pH 7.4.

b

. (ND) Not determined.