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Table 1 Biochemical Characteristics of wt BCMO1 and enzymatically active mutantsa.

From: Biochemical evidence for the tyrosine involvement in cationic intermediate stabilization in mouse β-carotene 15, 15'-monooxygenase

Enzyme

Km (μM)

Vmax

(pmol/μg*hour)

BCMO1wt

4.7

121.2

Y420F

3.6

109.9

Y418F

9.8

39.7

Y326W

20.1#

31.8

Y236F

15.4#

22.7

  1. aKm [μM] and Vmax [pmol retinal/hour* μg enzyme] were calculated from Hanes [s/v vs s] plots. Calculation of enzymatic activity was based on the production of retinal from β-carotene. Data was calculated based on average substrate curve for each protein.
  2. # These data are Km apparent values due to limitations of β-carotene solubility in reaction mixture (the highest concentration of β-carotene is 42 μM).