Tk. Ray et al., THE PRIMARY DEFECT IN DEVELOPING SEED FROM THE HIGH OLEATE VARIETY OFPEANUT (ARACHIS-HYPOGAEA L) IS THE ABSENCE OF BETA(12)-DESATURASE ACTIVITY, PLANT SCI, 91(1), 1993, pp. 15-21
A high oleate mutant variety of peanut, F435, has been identified whic
h has a seed oil containing 80% oleate and less than 2% linoleate (A.J
. Norden et al. Peanut Sci., 14 (1987) 7-11). This trait shows single
gene inheritance in some genetic backgrounds (K.M. Moore and D.A. Knau
ft, J. Hered., 80 (1989) 252-253). The DELTA12-desaturase is the enzym
e which catalyzes the conversion of oleate to linoleate, the first ste
p in the biosynthesis of polyunsaturated fatty acids. The high oleate
trait in variety F435 may result from a defect in this activity. In th
e present report, the DELTA12-desaturase activity in microsomes from d
eveloping peanut seed from the parent variety F78-1339 and the mutant
variety F435 are compared. The activity in developing peanut seed micr
osomes is unusually stable with a half-life of about 5 days at 0-degre
es-C. The specific activities of the supplementary components, 1-acyl-
2-lyso-sn-glycero(3)phosphocholine:acyl-CoA acyl transferase and cytoc
hrome b5 reductase and the concentrations of cytochrome b5, required f
or DELTA12-desaturase activity, were compared in normal and mutant mic
rosomes. These components were present in nearly equivalent concentrat
ions and activities. The high oleate trait in developing peanut seed v
ariety F435 is associated with a major decrease in the activity of the
DELTA12-desaturase with no changes in other activities associated wit
h the DELTA12-desaturase.