Activities | Families | Sequences | Fold types | References | Help
B6db references: 85280451

type Journal Article
authors Kelland, J. G.; Palcic, M. M.; Pickard, M. A.; Vederas, J. C.
title Stereochemistry of lysine formation by meso-diaminopimelate decarboxylase from wheat germ: use of 1H-13C NMR shift correlation to detect stereospecific deuterium labeling
journal Biochemistry
ui 85280451
year (1985)
volume 24
number 13
pages 3263-7.
keywords Carboxy-Lyases/*metabolism
abstract The stereochemical course of the wheat germ meso-diaminopimelate (DAP) decarboxylase reaction is compared to that of the decarboxylase isolated from Bacillus sphaericus, which has been reported to proceed with an unusual inversion of configuration [Asada, Y., Tanizawa, K., Sawada, S., Suzuki, T., Misono, H., & Soda, K. (1981) Biochemistry 20, 6881-6886]. Reaction of each enzyme with either unlabeled diaminopimelic acid in D2O or [2,6-2H2]diaminopimelic acid in H2O gave stereospecifically deuterium-labeled lysine samples that were derivatized with (-)-camphanoyl chloride and diazomethane. Analysis by two-dimensional 1H-13C heteronuclear NMR shift correlation spectroscopy with 2H decoupling confirmed the stereochemistry of the B. sphaericus enzyme reaction and showed that the eukaryotic wheat germ meso-DAP decarboxylase also operates with inversion of configuration. This suggests similar mechanisms for the prokaryotic and eukaryotic enzymes and contrasts the retention mode observed with other pyridoxal phosphate dependent alpha-decarboxylases.
last changed 2002/11/12 16:17

B6db references