Molybdopterin--problems and perspectives.

Abstract

Structural studies on several derivatives of molybdopterin, the organic component of the molybdenum cofactor common to virtually all molybdoenzymes, have provided definitive evidence for the presence of a reduced pterin ring with a 6-alkyl side-chain containing an enedithiol and a phosphomonoester in active molybdopterin. The cryptic nature of the cofactor makes structure - function studies on the protein-bound prosthetic group extremely difficult. In this review some of the relevant properties of the pterin ring are presented, and the possible roles of molybdopterin in catalysis are discussed.