The enzyme which catalyzes the adenosine triphosphatedependent addition of meso-,6-diaminopimelic acid to uridine diphosphate N-acetyhnuramyl-L-alanyl-D-glutamic acid has been purified from Bacillus cereus approximately 270-fold.The products of the reaction are uridine diphosphate N-acetyhnuramyl-L-alanyl-y-D-glutamyl-meso-2,6diaminopimelic acid, adenosine dlphosphate, and inorganic phosphate.The other optical isomers of 2,64aminopimelic acid, and L-lysine, fail to act as substrates.In addition to Mg++ or Mn++, I(+ or NH4+ is required in this reaction.The formation of adenosine triphosphate and 2,6-diaminopimelic acid in the reverse reaction catalyzed by this enzyme is demonstrated.
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Mizuno et al. (1968) studied this question.
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