Molybdopterin--problems and perspectives.
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.
Rajagopalan
K V
KV
Department of Biochemistry, Duke University Medical Center, Durham, NC 27710.
D003067:Coenzymes / Q000378:metabolism*; D008667:Metalloproteins / Q000378:metabolism*; D008982:Molybdenum / Q000378:metabolism*; D000090006:Molybdenum Cofactors; D011621:Pteridines / Q000378:metabolism*; D013329:Structure-Activity Relationship
D003067:Coenzymes; D008667:Metalloproteins; D008982:Molybdenum; D000090006:Molybdenum Cofactors; D011621:Pteridines; C022261:molybdopterin