Alanine racemase
![](/Images/godic/202412/18/PDB_1rcq_EBI4804.jpg")
![Figure 1. Active site of Alanine Racemase. Tyrosine-265 and Lysine-39 are displayed with their distances to the alpha-carbon of alanine, which is colored green and attached to PLP.](/Images/godic/202412/18/Alanine_Racemase_Active_Site4804.PNG")
![Figure 2. Surface Diagram of Alanine Racemase. The two monomers are colored in blue and green. The two reaction sites are colored in red.](/Images/godic/202412/18/Alanine_Racemase4804.PNG")
![Figure 3. Schematic diagram of the distance between Lys39, Tyr 265, and PLP-L-Ala in the active site. All interactions shown are under 4.5 and therefore are capable of hydrogen bonding. Adapted from Watanabe et al.](/Images/godic/202412/18/Distance_Between_Lys39,_Tyr_265,_and_PLP-L-Ala_in_the_Active_Site4804.PNG")
In enzymology, an alanine racemase (EC5.1.1.1) is an enzyme that catalyzes the chemical reaction
Hence, this enzyme has one substrate, L-alanine, and one product, D-alanine.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is alanine racemase. This enzyme is also called L-alanine racemase. This enzyme participates in alanine and aspartate metabolism and D-alanine metabolism. It employs one cofactor, pyridoxal phosphate. At least two compounds, 3-Fluoro-D-alanine and D-Cycloserine are known to inhibit this enzyme.