Comparison of the kinetic properties of MGDG synthase in mixed micelles and in envelope membranes from spinach chloroplast.
We have applied the 'membrane partition' kinetic modelling approach proposed by Heirwegh et al. [(1988) Biochem. J. 254, 101-108] to MGDG synthase in isolated envelope vesicles. Comparison of the kinetic parameters obtained for MGDG synthase assayed in purified envelope membranes and in mixed-micelles demonstrates that the latter are relevant to the situation in envelope membranes and that MGDG synthase has a very high affinity for dilinoleoylglycerol. Our results provide additional evidence for the hypothesis that the high affinity of the envelope MGDG synthase for dilinoleoylglycerol could be responsible for the presence of C18 fatty acids at both the sn-1 and sn-2 position of the glycerol backbone in MGDG.
Maréchal
E
E
Laboratoire de Physiologie Cellulaire Végétale, URA CNRS 576, Département de Biologie Moleculaire et Structurale, CEA-Centre d'Etudes Nucléaires de Grenoble, France.
Block
M A
MA
Joyard
J
J
Douce
R
R
D002458:Cell Fractionation; D002736:Chloroplasts / Q000201:enzymology* / Q000648:ultrastructure; D004075:Diglycerides / Q000494:pharmacology; D005700:Galactosyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D007425:Intracellular Membranes / Q000201:enzymology*; D007700:Kinetics; D008823:Micelles; D010713:Phosphatidylcholines; D010715:Phosphatidylglycerols; D018724:Spinacia oleracea / Q000201:enzymology
D004075:Diglycerides; D008823:Micelles; D010713:Phosphatidylcholines; D010715:Phosphatidylglycerols; D005700:Galactosyltransferases; C109990:1,2-diacylglycerol 3-beta-galactosyltransferase; C013965:diolein