Steve Ealick's Research Group

E-2-(Acetamidomethylene)succinate Hydrolase

PDB file:



E-2-(acetamidomethylene)succinate (E-2AMS) hydrolase is the last enzyme to be biochemically characterized on the vitamin B6 catabolic pathway. This enzyme, found in Mesorhizobium loti MAFF30309, catalyzes the hydrolysis of E-2AMS to succinic semialdehyde, ammonia, acetate, and carbon dioxide.

The overall fold of this enzyme indicates that E-2AMS hydrolase belongs to the α/β hydrolase superfamily despite a low sequence identity to thisfamily of enzymes.

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The two protomers in the biologically relevant dimer are related to each other by local twofold symmetry. The β-sheets of each chain face in the same direction, but twist in opposite directions.

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Although all attempts at cocrystallization or soaking E-2AMS into crystals of E-2AMS hydrolase were unsuccessful, examination of the active site suggests several residues that could play important roles in both the binding of E-2AMS. The figure at right shows


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McCulloch KM, Mukherjee T, Begley TP, and Ealick SE. Structure Determination and Characterization of the Vitamin B6 Degradative Enzyme (E)-2-(Acetamidomethylene)Succinate Hydrolase. Biochemistry 49: 1226-1235 (2010).

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