An enzyme has been isolated from wheat germ which catalyzes the reaction: ADP-sugar + inorganic phosphate → ADP + sugar phosphate. Maximal activity was found at pH 8-9. The equilibrium of the reaction seems to be completely displaced towards ADP formation. The enzyme acts on ADP-glucose and deADP-glucose and more slowly, on ADP-xylose and ADP-β-glucose. Evidence is presented indicating that inorganic phosphate is incorporated in the terminal position of the nucleotide. Arsenate can be substituted for inorganic phosphate, AMP being the final product. © 1964.
Documento: | Artículo |
Título: | Adenosine diphosphate glucose: Orthophosphate adenylyltransferase in wheat germ |
Autor: | Dankert, M.; Ruth, I.; Gonçalves, J.; Recondo, E. |
Filiación: | Instituto de Investigaciones Bioquimicas Fundación Campomar, Facultad de Ciencias Exactas y Naturales, Obligado 2490 Buenos Aires, Argentina |
Año: | 1964 |
Volumen: | 81 |
Número: | 1 |
Página de inicio: | 78 |
Página de fin: | 85 |
DOI: | http://dx.doi.org/10.1016/0926-6569(64)90337-2 |
Título revista: | BBA - Enzymological Subjects |
ISSN: | 09266569 |
Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09266569_v81_n1_p78_Dankert |