|
type |
Journal Article |
authors |
Momany, C.; Levdikov, V.; Blagova, L.; Crews, K. |
title |
Crystallization of diaminopimelate decarboxylase from Escherichia coli, a stereospecific D-amino-acid decarboxylase |
journal |
Acta Crystallogr D Biol Crystallogr |
Activity |
4.1.1.20 |
ui |
21845121 |
year |
(2002) |
volume |
58 |
number |
Pt 3 |
pages |
549-52. |
| |
keywords |
Carboxy-Lyases/*chemistry/genetics |
abstract |
The final step in lysine biosynthesis in bacteria, the conversion of meso-diaminopimelate to L-lysine, is catalyzed by the only known D- amino-acid decarboxylase, diaminopimelate decarboxylase (DDC). The Escherichia coli DDC has been cloned, overexpressed in E. coli with a carboxy-terminal polyhistidine purification tag and crystallized from lithium sulfate. The protein is intensely yellow, owing to the pyridoxal-5'-phosphate cofactor, and is enzymatically active. Large well ordered crystals, belonging to space group P6(1)22 with unit-cell parameters a = b = 98.6, c = 177 A, make high-resolution X-ray diffraction studies possible to characterize the residues important in stereospecific decarboxylation and reprotonation during catalytic turnover. |
last changed |
2002/11/12 16:17 |
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