Structural and biochemical characterization of the biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminasorum bv. viciae 3841
Fig 7
The active site of the Lys142Ala variant of BiuH showing Cys175 bound to the inhibitor N-carbamoyl-D,L-aspartic acid.
BiuH is represented in cartoon style, with the exception of the active site amino acids; N-carbamoyl-D,L-aspartic acid is shown in pink, the hydrogen bond between the Gln215 and N-carbamoyl-D,L-aspartic acid are shown in grey, the hydrogen bonds between Asp36 and Ala142 in red; Gln215 is shown in cyan as it belongs to another enzyme subunit. The inhibition profile of BiuH with N-carbamoyl-D,L-aspartic acid is shown in S5 Fig and the difference density map (Fo −Fc) of the covalently bound inhibitor is shown in S11 Fig.