Two‐Metal Ion Catalysis in Enzymatic Acyl‐ and Phosphoryl‐Transfer Reactions

摘要: Numerous studies, both in enzymatic and nonenzymatic catalysis, have been undertaken to understand the way by which metal ions, especially zinc promote hydrolysis of phosphate ester amide bonds. Hydrolases containing one ion active site, termed mononuclear metallohydrolases, such as carboxypeptidase. A thermolysin were among first enzymes their structures unraveled X-ray crystallography. In recent years an increasing number metalloenzymes identified that use two or more adjacent ions catalysis phosphoryl-transfer reactions (R-OPO3 + R′-OH R′-OPO3 R-OH; case phosphatase reaction is a water molecule) carbonyl-transfer reactions, for example, peptidases other amidases. These dinuclear catalyze great variety these including hydrolytic cleavage phosphomono-, -di- -triester bonds, phosphoanhydride bonds well peptide urea. addition, formation phosphodiester bond RNA DNA polymerases catalyzed two-metal mechanism. remarkable diversity also seen sites di- trinuclear metalloenzymes, even very similar reactions. The determination structure substrate, product, stable intermediate, coordinate analogue compound bound inactivated enzyme powerful approach investigate mechanistic details action. Such studies applied several reviewed this article; together with many biochemical they provide growing body information on how (or more) cooperate achieve efficient catalysis.