Mammalian flavokinase and FAD synthetase: functions of divalent metal ions and arginyl residues in the anionic substrate sites.
Nakano
H
H
Department of Biochemistry, Emory University, Atlanta, GA 30322.
Hartman
H A
HA
McCormick
D B
DB
D000255:Adenosine Triphosphate / Q000737:chemistry; D000818:Animals; D000838:Anions; D001120:Arginine / Q000737:chemistry*; D001665:Binding Sites / Q000502:physiology; D002413:Cations, Divalent; D008670:Metals / Q000737:chemistry*; D009713:Nucleotidyltransferases / Q000737:chemistry*; D010770:Phosphotransferases / Q000737:chemistry*; D017853:Phosphotransferases (Alcohol Group Acceptor); D015032:Zinc / Q000737:chemistry
D000838:Anions; D002413:Cations, Divalent; D008670:Metals; D000255:Adenosine Triphosphate; D001120:Arginine; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C022532:riboflavin kinase; D009713:Nucleotidyltransferases; C020143:FMN adenylyltransferase; D015032:Zinc