Transglucosidation reactions with flavins
- 1 July 1954
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 57 (3) , 390-396
- https://doi.org/10.1042/bj0570390
Abstract
The specificity of the enzyme which synthesizes ribo-flavinyl glucoside was investigated in an attempt to assess the physiological significance of this derivative of riboflavin. It is possible that the enzyme has both transglucosidase and glu-cosidase activities. The transglucosidase synthesizes gluco-sides of several isoalloxazine derivatives, many of which are antivitamins. Certain specificity requirements were defined for the glucose donor and for the flavin acceptor. The quantitative characteristics of the formation of riboflavinyl glucoside from riboflavin and maltose were investigated, and the inhibition of this reaction by alpha-D-glucose 1-phosphate was shown to be competitive. The solubility of riboflavinyl glucoside in water is much greater than the solubility of riboflavin, and it is suggested that this may be of importance in the transport of riboflavin.Keywords
This publication has 10 references indexed in Scilit:
- Mould ‘glucosaccharase’: a fructosidaseBiochemical Journal, 1953
- The action of mould enzymes on sucroseBiochemical Journal, 1953
- THE INTERACTION OF YEAST FLAVOKINASE WITH RIBOFLAVIN ANALOGUESJournal of Biological Chemistry, 1952
- Riboflavinyl glucoside: a new derivative of riboflavinBiochemical Journal, 1952
- Transfructosidation by a yeast invertase preparation.1952
- The L-amino acid oxidases of snake venom; prosthetic group of the L-amino acid oxidase of moccasin venom.1950
- THE FLUOROMETRIC MEASUREMENT OF THE NUCLEOTIDES OF RIBOFLAVIN AND THEIR CONCENTRATION IN TISSUESJournal of Biological Chemistry, 1949
- Crystalline Derivatives of IsomaltoseJournal of the American Chemical Society, 1949
- Iso‐alloxazinderivate als Antagonisten des RiboflavinsHelvetica Chimica Acta, 1946
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934