Structures of an alanine racemase from Bacillus anthracis (BA0252) in the presence and absence of (R)-1-aminoethylphosphonic acid (l-Ala-P)

Au, K.; Ren, J.; Walter, T.S.; Harlos, K.; Nettleship, J.E.; Owens, R.J.; Stuart, D.I.; Esnouf, R.M.

doi:10.1107/S1744309108007252

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 1
The classical two-base mechanism of the reaction catalyzed by alanine racemase using pyridoxal 5′-phosphate as a cofactor. The reaction is shown in the direction of conversion from L-alanine to D-alanine, in which Tyr270′ abstracts a proton from L-alanine to form a planar intermediate and Lys41 donates a proton to form D-alanine. A more detailed mechanism avoiding the creation of a quinonoid intermediate has been proposed by Watanabe et al. (2002

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 64| Part 5| April 2008| Pages 327-333

doi:10.1107/S1744309108007252

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