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. 2010 Jul 14;285(39):30181–30191. doi: 10.1074/jbc.M110.120329

TABLE 1.

Kinetic properties of Cyb5A/Cyb5R3 and Ncb5or-b5/Ncb5or-b5R reduction

The raw data of V0 versus [S] were fit to the Michaelis-Menten equation to generate Km and kcat (Vmax/[E]). The substrate is either Cyb5A or Ncb5or-b5, and the enzyme is either Cyb5R3 or Ncb5or-b5R.

Substrate/Enzyme [E] Km kcat kcat/Km
nm μm s1 μm1s1
Cyb5A/Cyb5R3 0.56 7.6 ± 0.3 230 ± 3 30.1
Ncb5or-b5/ Ncb5or-b5R 140 498 ± 129 8.8 ± 1.9 0.018