Conversion of neutral to alkaline liver fructose 1,6-bisphosphatase: changes in molecular properties of the enzyme
- PMID: 4351799
- PMCID: PMC433329
- DOI: 10.1073/pnas.70.3.661
Conversion of neutral to alkaline liver fructose 1,6-bisphosphatase: changes in molecular properties of the enzyme
Abstract
Removal of the NH(2)-terminal region of fructose 1,6-bisphosphatase from rabbit liver by digestion with subtillisin, or changes in conformation in this region of the protein produced by exposure to low concentrations of urea, result in similar changes in catalytic and allosteric properties of the enzyme. These changes include shift of the pH optimum to more alkaline pH, and loss of sensitivity to inhibition by AMP. The conformation changes are monitored by changes in the fluorescence of the single tryptophan residue, which is located near the NH(2)-terminus. Thus, the tryptophan-containing peptide appears to determine the functional properties of the native enzyme.
Similar articles
-
Cooperative interactions between native and modified subunits of rabbit liver fructose 1,6-bisphosphatase.Arch Biochem Biophys. 1974 Aug;163(2):435-41. doi: 10.1016/0003-9861(74)90499-8. Arch Biochem Biophys. 1974. PMID: 4369889 No abstract available.
-
Structural changes of rabbit liver fructose-1,6-bisphosphatase: the effect of urea and subtilisin digestion.Arch Biochem Biophys. 1985 Jun;239(2):486-90. doi: 10.1016/0003-9861(85)90716-7. Arch Biochem Biophys. 1985. PMID: 2988451
-
Relationship between thiol group modification and the binding site for fructose 2,6-bisphosphate on rabbit liver fructose-1,6-bisphosphatase.J Biol Chem. 1988 Jul 15;263(20):10035-9. J Biol Chem. 1988. PMID: 2838468
-
Fructose 1,6-bisphosphatase: properties of the neutral enzyme and its modification by proteolytic enzymes.Adv Enzymol Relat Areas Mol Biol. 1975;42:193-226. doi: 10.1002/9780470122877.ch4. Adv Enzymol Relat Areas Mol Biol. 1975. PMID: 236638 Review. No abstract available.
-
Control of hepatic fructose-metabolizing enzymes: fructokinase, aldolase and triokinase.Acta Med Scand Suppl. 1972;542:47-56. doi: 10.1111/j.0954-6820.1972.tb05318.x. Acta Med Scand Suppl. 1972. PMID: 4579754 Review. No abstract available.
Cited by
-
Changes in activity and molecular properties of fructose 1, 6-bisphosphatase during fasting and refeeding.Proc Natl Acad Sci U S A. 1974 May;71(5):1776-9. doi: 10.1073/pnas.71.5.1776. Proc Natl Acad Sci U S A. 1974. PMID: 4365572 Free PMC article.
-
Biochemical observations on a case of hepatic fructose-1,6-diphosphatase deficiency.J Inherit Metab Dis. 1985;8(4):169-73. doi: 10.1007/BF01805428. J Inherit Metab Dis. 1985. PMID: 3023747
-
Changes in rabbit-liver lysosomes and fructose 1,6-bisphosphatase induced by cold and fasting.Proc Natl Acad Sci U S A. 1973 Dec;70(12):3674-8. doi: 10.1073/pnas.70.12.3674. Proc Natl Acad Sci U S A. 1973. PMID: 4357886 Free PMC article.
-
The chymotrypsin-catalysed activation of bovine liver glutamate dehydrogenase.Biochem J. 1982 Jul 1;205(1):75-80. doi: 10.1042/bj2050075. Biochem J. 1982. PMID: 7126185 Free PMC article.
-
Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium.Proc Natl Acad Sci U S A. 1990 Jul;87(14):5243-7. doi: 10.1073/pnas.87.14.5243. Proc Natl Acad Sci U S A. 1990. PMID: 2164670 Free PMC article.
References
MeSH terms
Substances
LinkOut - more resources
Full Text Sources