Premium
Comparison of the kinetic properties of MGDG synthase in mixed micelles and in envelope membranes from spinach chloroplast
Author(s) -
Maréchal Eric,
Block Maryse A.,
Joyard Jacques,
Douce Roland
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00978-3
Subject(s) - membrane , vesicle , atp synthase , micelle , chemistry , spinach , chloroplast membrane , biochemistry , kinetics , biophysics , chloroplast , thylakoid , enzyme , biology , organic chemistry , physics , quantum mechanics , aqueous solution , gene
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.