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B6db references: 21845121

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
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

B6db references