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J Biosci Bioeng. 2003;96(2):103-9.

Amino acid racemases: functions and mechanisms.

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Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.


L-Amino acids are predominant in living organisms, but D-amino acids such as D-alanine and D-glutamate also occur in all eubacterial cell walls. Moreover, even mammals contain endogenous D-amino acids: D-serine functions as a signaling molecule in mammalian brains, and D-aspartate acts as a mediator in endocrine systems. Various other D-amino acids have been demonstrated in archaea, yeasts, fungi, plants, insects, mollusks and other eucaryotic organisms. These D-amino acids are mostly endogenous and produced in most cases by racemization from their corresponding antipodes by the action of racemases. Therefore, amino acid racemases play a central role in D-amino acid metabolism. Most amino acid racemases require pyridoxal 5'-phosphate (PLP) as a coenzyme, but several others require no coenzymes. Recently, the structures and functions of these two classes of amino acid racemases were clarified on a molecular basis. We here describe recent advances in studies of the functions and mechanisms of PLP-dependent and -independent amino acid racemases.


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