Abstract:
:Rat liver fructose 1,6-bisphosphatase can be protected against partial inactivation by N-ethylmaleimide by low concentrations of fructose 2,6-bisphosphate or high concentrations of fructose 1,6-bisphosphate. The partially inactivated enzyme has a much reduced sensitivity to high substrate inhibition and has lost the sigmoid component of the inhibition by fructose 2,6-bisphosphate; this compound is a simple linear competitive inhibitor of the modified enzyme. The results suggest that fructose 2,6-bisphosphate can bind to the enzyme at two distinct sites, the catalytic site and an allosteric site. High levels of fructose 1,6-bisphosphate probably inhibit by binding to the allosteric site.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Meek DW,Nimmo HGdoi
10.1016/0014-5793(83)80946-6subject
Has Abstractpub_date
1983-08-22 00:00:00pages
105-9issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(83)80946-6journal_volume
160pub_type
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