Structural highlights
Function
DCDA_ECOLI Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. Is not active against the DD- or LL-isomers of diaminopimelate.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ WHITE PJ, KELLY B. PURIFICATION AND PROPERTIES OF DIAMINOPIMELATE DECARBOXYLASE FROM ESCHERICHIA COLI. Biochem J. 1965 Jul;96:75-84. PMID:14343156
- ↑ Momany C, Levdikov V, Blagova L, Crews K. Crystallization of diaminopimelate decarboxylase from Escherichia coli, a stereospecific D-amino-acid decarboxylase. Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):549-52. Epub 2002 Feb 21. PMID:11856852
- ↑ Hu T, Wu D, Chen J, Ding J, Jiang H, Shen X. The catalytic intermediate stabilized by a "down" active site loop for diaminopimelate decarboxylase from Helicobacter pylori. Enzymatic characterization with crystal structure analysis. J Biol Chem. 2008 Jul 25;283(30):21284-93. Epub 2008 May 28. PMID:18508763 doi:http://dx.doi.org/10.1074/jbc.M801823200
