Fructose 1,6-Bisphosphatase: The Role of Lysosomal Enzymes in the Modification of Catalytic and Structural Properties
AUTOR(ES)
Pontremoli, S.
RESUMO
Seasonal variations in the properties of rabbit-liver fructose 1,6-bisphosphatase have now been linked to corresponding changes in the levels of proteolytic activity in the liver extracts. Incubation of native fructose 1,6-bisphosphatase with purified liver lysosomes causes a 3-fold increase in catalytic activity at pH 9.2, with a smaller, and variable, decrease in activity tested at pH 7.5. These changes in catalytic properties are accompanied by the appearance of a smaller subunit, as was previously reported for the enzyme treated with subtilisin. AMP, a negative modulator of fructose bisphosphatase activity, protects against this action of lysosomes. This proteolytic modification of fructose bisphosphatase by lysosomal enzymes may play a role in the modulation of gluconeogenesis.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=433244Documentos Relacionados
- Conversion of Neutral to Alkaline Liver Fructose 1,6-Bisphosphatase: Changes in Molecular Properties of the Enzyme
- Hormonal effects on structure and catalytic properties of fructose 1,6-bisphosphatase.
- Binding of Zn2+ to rat liver fructose-1,6-bisphosphatase and its effect on the catalytic properties.
- Chemical modification of the allosteric and catalytic sites of fructose 1,6-diphosphatase.
- Changes during fasting in the activity of a specific lysosomal proteinase, fructose-1,6-bisphosphatase converting enzyme.
