A protein identified as “N-acylamino acid racemase” from Amycolaptosis sp. is an inefficient
enzyme (k cat/K m= 3.7× 102 M-1 s-1). Its sequence is 43% identical to that of an …

Understanding how proteins evolve to provide both exquisite specificity and proficient
activity is a fundamental problem in biology that has implications for protein function …

o-Succinylbenzoate synthase (OSBS) from Amycolatopsis, a member of the enolase
superfamily, catalyzes the Mn2+-dependent exergonic dehydration of 2-succinyl-6 R …

Divergent evolution of enzyme function is commonly explained by a gene duplication event
followed by mutational changes that allow the protein encoded by the copy to acquire a new …

The X-ray structures of the ligand free (apo) and the Mg2+• o-succinylbenzoate (OSB)
product complex of o-succinylbenzoate synthase (OSBS) from Escherichia coli have been …

Members of the mechanistically diverse enolase superfamily catalyze reactions that are
initiated by abstraction of the α-proton of a carboxylate anion to generate an enolate anion …

o-Succinylbenzoate synthase (OSBS) from Escherichia coli, a member of the enolase
superfamily, catalyzes an exergonic dehydration reaction in the menaquinone biosynthetic …

We have discovered a superfamily of enzymes related by their ability to catalyze the
abstraction of the α-proton of a carboxylic acid to form an enolic intermediate. Although each …

Enzyme catalysis reflects a dynamic interplay between charged and polar active site
residues that facilitate function, stabilize transition states, and maintain overall protein …

The members of the mechanistically diverse enolase superfamily catalyze different overall
reactions by using a common catalytic strategy and structural scaffold. In the muconate …