Table III.
Substrate | Relative Activity | Km value | Vmax | Vmax/Km |
---|---|---|---|---|
%c | μm | pkat mg−1 | ||
Q | 100 | 12 | 61 | 5.08 |
Kaempferol | 93 | 13 | 169 | 13 |
Myricetin | 46 | 7 | 15 | 2.14 |
The enzyme protein fraction II eluted from the Mono-Q column (Fig. 3A) was assayed against the indicated substrates at a concentration of 50 μm as described in “Materials and Methods”.
See Figure 1 for structures of the substrates used.
No OMT activity was detected with either catechol, caffeic acid, caffeoyl CoA, or 3-MeQ, nor with naringenin, eriodyctiol, apigenin, or luteolin when used as substrates. Other substrates were accepted to varying degrees (% of control); these are: isorhamnetin (88%), tamarixetin (85%), herbacetin (33%), rhamnetin (13%), galangin (60%), quercetagetin (39%), and gossypetin (38%).
Equivalent to a specific activity of 3.26 pkat g−1.