Flavoenzymes that catalyse reactions with no net redox change.
This review covers unusual flavoenzymes that catalyse reactions with no net redox change. Some of these enzymes utilise the redox properties of flavin directly in catalysis with either two-electron chemistry (N-methylglutamate synthase and 5-hydroxyvaleryl-CoA dehydratase) or free radical chemistry (chorismate synthase, DNA photolyase, (6-4) photolyase and 4-hydroxybutyryl-CoA dehydratase). Whether the flavin has a redox role in some other flavoproteins is not yet clear ((R)-2-hydroxyacyl-CoA dehydratases, isopentenyl diphosphate isomerase and UDPgalactopyranose mutase). The remaining flavoenzymes do not make use of the redox properties of the flavin (acetohydroxyacid synthases and hydroxynitrile lyase). The literature is reviewed up to early 2002 and 121 references are cited.
Bornemann
Stephen
S
Department of Biological Chemistry, John Innes Centre, Norwich, UK NR4 7UH. stephen.bornemann@bbsrc.ac.uk
D002384:Catalysis; D004255:Deoxyribodipyrimidine Photo-Lyase / Q000378:metabolism; D004798:Enzymes / Q000378:metabolism*; D005415:Flavins / Q000378:metabolism; D005420:Flavoproteins / Q000378:metabolism*; D015394:Molecular Structure; D010084:Oxidation-Reduction; D019761:Phosphorus-Oxygen Lyases / Q000378:metabolism
D004798:Enzymes; D005415:Flavins; D005420:Flavoproteins; D004255:Deoxyribodipyrimidine Photo-Lyase; C019895:chorismate synthase; D019761:Phosphorus-Oxygen Lyases