New Targets for Antibacterial Agent——Alanine Racemase

LIUXiao-Qin,SHIYa-Wei

Chinese Journal of Biochemistry and Molecular Biology ›› 2010, Vol. 26 ›› Issue (02) : 104-108.

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PDF(712 KB)
Chinese Journal of Biochemistry and Molecular Biology ›› 2010, Vol. 26 ›› Issue (02) : 104-108.
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New Targets for Antibacterial Agent——Alanine Racemase

  • LIU Xiao-Qin, SHI Ya-Wei*
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Abstract

Alanine racemase (AlaR) is a pyridoxal 5′-phosphate (PLP)-dependent enzyme that catalyzes the interconversion of L- and D-alanine isomers. AlaR belong to the fold-type Ⅲ group of PLP-dependent enzymes. It is ubiquitously existed and highly conserved in bacteria, but is generally absent in human and higher eukaryotes. The AlaR functioned mostly as homodimers comprised of two identical catalytic active sites which contained two conserved residues each from different monomers. AlaR plays an important role in the bacterial growth to provide D-alanine, a key molecule in the peptidyl-glycan assembly and crosslinking and an essential factor to modulate bacterial spore germination. AlaR is also associated with human diseases, such as tuberculosis, anthrax, and otitis, therefore can be regarded as an potential target for the design of new antibacterial drugs. In this review, the recent advances in alanine racemases tudies with the aspects of structure, function, mechanism, and inhibitors will be discussed.

Key words

wordsalanine racemase / structure / mechanism / function / diseases

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LIUXiao-Qin,SHIYa-Wei. New Targets for Antibacterial Agent——Alanine Racemase[J]. Chinese Journal of Biochemistry and Molecular Biology, 2010, 26(02): 104-108

References

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