Electron-transferring flavoprotein from pig and the methylotrophic bacterium W3A1 contains AMP as well as FAD.
Electron-transferring flavoproteins from pig kidney and from the methylotrophic bacterium W3A1 have been found to contain one molecule of AMP in addition to the single FAD molecule bound to these heterodimers. The nucleotide was identified by spectral and chromatographic methods and via its behavior toward adenylate kinase and alkaline phosphatase. The role of this additional non-redox active prosthetic group in electron transferring-flavoprotein is at present unclear.
Department of Chemistry and Biochemistry, University of Delaware, Newark 19716.
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DuPlessis
R J
RJ
Rohlfs
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R
Hille
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Thorpe
D000249:Adenosine Monophosphate / Q000032:analysis; D000263:Adenylate Kinase / Q000378:metabolism; D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D004579:Electron Transport; D005182:Flavin-Adenine Dinucleotide / Q000032:analysis; D005420:Flavoproteins / Q000737:chemistry*; D007668:Kidney / Q000737:chemistry; D008772:Methylococcaceae / Q000737:chemistry*; D011108:Polymers; D013056:Spectrophotometry, Ultraviolet; D013552:Swine
D005420:Flavoproteins; D011108:Polymers; D005182:Flavin-Adenine Dinucleotide; D000249:Adenosine Monophosphate; D000263:Adenylate Kinase; D000469:Alkaline Phosphatase