A.e-Diaminopimelate decarboxylase

Meso-a, e-diaminopimelate decarboxylase Bacillus sphaericus, wheat germ DL-Diaminopimelate Inversion 259, 260... 

Nevertheless, an exception to the general rule of retention has recently been discovered in the form of mcfo-a,e-diaminopimelate decarboxylase from Bacillus sphaerkus (259). This PLP-dependent enzyme, which catalyzes the final step in lysine biosynthesis, is the only known amino acid decarboxylase to operate on an a-carbon having the D-configuiation (264). Inversion of configuration was demonstrated for the enzyme from Bacillus sphaerkus by conducting the decarboxylation reaction in H20 solvent and isolating as product (6I7)-l-[6-2H]lysine [Eq. (50)] ... 

The stereochemistry of meso-a,e-diaminopimelate decarboxylase from a eukaryotic source (wheat germ) also involves inversion of configuration (260). As suggested by Floss and Vederas inversion might be comprehensible if the enzyme evolved from a preexisting L-amino acid decarboxylase in which the dispositions... 

The enzyme a,E-diaminopimelate decarboxylase (EC 4.1.1.20) decar-boxylates the (R) center of (25,6/ )-ffieso-diaminopimelic acid 262 to give lysine 257a (Scheme 69). When this reaction was conducted in and... 

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See also in sourсe #XX -- [ ]

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