Structure and mechanism of tryptophylquinone enzymes.
Tryptophylquinone cofactors are formed by posttranslational modifications that result in the incorporation of two oxygens into a tryptophan side chain, and the covalent cross-linking of that side chain to another amino acid residue. Tryptophylquinone enzymes catalyze the oxidative deamination of primary amines, and utilize other redox proteins as electron acceptors. Mechanistic and structural studies of these enzymes are providing insight into how these enzymes utilize these highly reactive protein-derived quinones in a controlled manner to facilitate biologically important catalytic and electron transfer reactions.
Davidson
Victor L
VL
Department of Biochemistry, The University of Mississippi Medical Center, 2500 N. State St., Jackson, MS 39216-4505, USA. vdavidson@biochem.umsmed.edu
D002384:Catalysis; D018360:Crystallography, X-Ray; D004579:Electron Transport; D045563:Indolequinones / Q000737:chemistry*; D008958:Models, Molecular; D010084:Oxidation-Reduction; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry* / Q000502:physiology; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D014364:Tryptophan / Q000031:analogs & derivatives* / Q000737:chemistry
D045563:Indolequinones; C070569:tryptophan tryptophylquinone; D014364:Tryptophan; D000587:Oxidoreductases Acting on CH-NH Group Donors