 Fumarase C

Fumarase C, often designated FumC, is a classII form of fumarate hydratase. It catalyzes reversible hydration of fumarate to L-malate. The protein designation should be tied to an organism: Escherichia coli fumarase C is a well-studied species-specific example, while the broader enzyme-activity name does not specify one protein sequence.^[ref]

The net substrate inventory makes the chemistry explicit:Four carbon atoms remain four; adding water changes hydrogen and oxygen content without changing the total charge. This hydration is chemically distinct from oxidation of L-malate to oxaloacetate. The enzyme accelerates a reversible reaction rather than making its net direction independent of conditions.^[ref]

The1995 X-ray crystallography study of the E.coli enzyme resolved an assembly of four identical protein subunits at2.0Å. Its proposed active site involved contributions from three of the four protein subunits; a local catalytic environment therefore need not lie inside just one polypeptide chain. A1996 follow-up with bound compounds distinguished the catalytic A-site from a nearby second binding site. These experiments also show why observing ligand binding does not by itself identify a catalytic site.^[ref][ref]