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- W1650862541 abstract "Publisher Summary This chapter describes the assay method and properties of the riboflavin hydrolase enzyme prepared from Pseudomonas riboflavin . The disappearance of flavin, usually riboflavin, during the reaction is assayed fluorometrically. By use of riboflavin-2- 14 C, both the disappearance of riboflavin and appearance of lumichrome are determined by measuring the radioactivities after their separation by paper chromatography. The enzyme is prepared from P. riboflavin that is cultured aerobically for 24 hours at 30°C on a riboflavin–yeast–salts medium. The enzyme does not function under anaerobic conditions and is inhibited by higher levels of substrate. Inorganic phosphate or ATP is not involved in the reaction. The substrate specificity of this bacterial enzyme is reviewed. The system is more reactive toward a 9-D-ribityl side chain as by the lower substrate reactivities of the flavins with substituents on the 9-position of the isoalloxazine ring system." @default.
- W1650862541 created "2016-06-24" @default.
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- W1650862541 date "1971-01-01" @default.
- W1650862541 modified "2023-09-27" @default.
- W1650862541 title "[164] Riboflavin hydrolase (EC 3.5.99.1) from Pseudomonas riboflavina" @default.
- W1650862541 cites W172094791 @default.
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- W1650862541 doi "https://doi.org/10.1016/s0076-6879(71)18121-9" @default.
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