|
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 |
Activity |
4.1.1.20 |
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 |
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