Altered feedback sensitivity of acetohydroxyacid synthase from valine-resistant mutants of tobacco (Nicotiana tabacum L.).
Acetohydroxyacid synthase (EC 4.1.3.18) has been extracted from leaves of three valine-resistant (Val(r)) tobacco (Nicotiana tabacum) mutants, and compared with the enzyme from the wild-type. The enzyme from all three mutants is appreciably less sensitive to inhibition by leucine and valine than the wild-type. Two of the mutants, Val(r)-1 and Val(r)-6, have very similar enzymes, which under all conditions are inhibited by less than half that found for the wild-type. The other mutant, Val(r)-7, has an enzyme that only displays appreciably different characteristics from the wild-type at high pyruvate or inhibitor concentrations. Enzyme from Val(r)-7 also has a higher apparent Km for pyruvate, threefold greater than the value determined for the wild-type and the other mutants. The sulphonylurea herbicides strongly inhibit the enzyme from all the lines, though the concentrations required for half-maximal inhibition of enzyme from Val(r)-1 and Val(r)-6 are higher than for Val(r)-7 or the wildtype. No evidence has been found for multiple isoforms of acetohydroxyacid synthase, and it is suggested that the valine-resistance of these mutant lines is the result of two different mutations affecting a single enzyme, possibly involving different subunits.
Biochemistry Department, Rothamsted Experimental Station, AL5 2JQ, Harpenden, Herts, UK.
J M
JM
Relton
R M
RM
Wallsgrove
J P
JP
Bourgin
S W
SW
Bright