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Literature DB >> 4351799

Conversion of neutral to alkaline liver fructose 1,6-bisphosphatase: changes in molecular properties of the enzyme.

S Pontremoli, E Melloni, A De Flora, B L Horecker.

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.

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Year: 1973 PMID： 4351799 PMCID： PMC433329 DOI： 10.1073/pnas.70.3.661

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

10 in total

1. ALTERATION OF ENZYMATIC ACTIVITIES OF RAT LIVER DIPHOSPHATASE BY TREATMENT WITH PAPAIN OR UREA.

Authors: G MANGIAROTTI; S PONTREMOLI
Journal: Biochem Biophys Res Commun Date: 1963-08-01 Impact factor: 3.575

2. Protein measurement with the Folin phenol reagent.

Authors: O H LOWRY; N J ROSEBROUGH; A L FARR; R J RANDALL
Journal: J Biol Chem Date: 1951-11 Impact factor: 5.157

3. Fructose 1, 6-diphosphatase from liver: isolation of the native form with optimal activity at neutral pH.

Authors: S Traniello; S Pontremoli; Y Tashima; B L Horecker
Journal: Arch Biochem Biophys Date: 1971-09 Impact factor: 4.013

4. Rabbit liver fructose 1,6-diphosphatase. Properties of the native enzyme and their modification by subtilisin.

Authors: S Traniello; E Melloni; S Pontremoli; C L Sia; R L Horecker
Journal: Arch Biochem Biophys Date: 1972-03 Impact factor: 4.013

5. Chemical modification of the allosteric and catalytic sites of fructose 1,6-diphosphatase.

Authors: O M Rosen; S M Rosen
Journal: Proc Natl Acad Sci U S A Date: 1966-05 Impact factor: 11.205

6. Fructose diphosphatase from rabbit liver. II. Changes in catalytic properties induced by dinitrofluorobenzene.

Authors: S Pontremoli; B Luppis; W A Wood; S Traniello; B L Horecker
Journal: J Biol Chem Date: 1965-09 Impact factor: 5.157

7. Fructose diphosphatase from rabbit liver. 3. Nature of the groups reactive with dinitrofluorobenzene.

Authors: S Pontremoli; B Luppis; S Traniello; W A Wood; B L Horecker
Journal: J Biol Chem Date: 1965-09 Impact factor: 5.157

8. The carboxyl-terminal structure of rabbit liver aldolase (aldolase B).

Authors: A G Lacko; L W Brox; R W Gracy; B L Horecker
Journal: J Biol Chem Date: 1970-04-25 Impact factor: 5.157

9. The tryptophan microenvironments in apomyoglobin.

Authors: E P Kirby; R F Steiner
Journal: J Biol Chem Date: 1970-12-10 Impact factor: 5.157

10. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.

Authors: K Weber; M Osborn
Journal: J Biol Chem Date: 1969-08-25 Impact factor: 5.157

10 in total

8 in total

Conversion of neutral to alkaline liver fructose 1,6-bisphosphatase: changes in molecular properties of the enzyme.

1. ALTERATION OF ENZYMATIC ACTIVITIES OF RAT LIVER DIPHOSPHATASE BY TREATMENT WITH PAPAIN OR UREA.

2. Protein measurement with the Folin phenol reagent.

3. Fructose 1, 6-diphosphatase from liver: isolation of the native form with optimal activity at neutral pH.

4. Rabbit liver fructose 1,6-diphosphatase. Properties of the native enzyme and their modification by subtilisin.

5. Chemical modification of the allosteric and catalytic sites of fructose 1,6-diphosphatase.

6. Fructose diphosphatase from rabbit liver. II. Changes in catalytic properties induced by dinitrofluorobenzene.

7. Fructose diphosphatase from rabbit liver. 3. Nature of the groups reactive with dinitrofluorobenzene.

8. The carboxyl-terminal structure of rabbit liver aldolase (aldolase B).

9. The tryptophan microenvironments in apomyoglobin.

10. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.

1. Hormonal effects on structure and catalytic properties of fructose 1,6-bisphosphatase.

2. Biochemical observations on a case of hepatic fructose-1,6-diphosphatase deficiency.

3. Regulation of fructose, 1,6-bisphosphatase by histidine under gluconeogenic conditions.

4. The chymotrypsin-catalysed activation of bovine liver glutamate dehydrogenase.

5. The purification of fructose 1,6-diphosphatase from ox liver and its activation by ethylenediaminetetra-acetate.

6. Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium.

7. Changes in rabbit-liver lysosomes and fructose 1,6-bisphosphatase induced by cold and fasting.

8. Changes in activity and molecular properties of fructose 1, 6-bisphosphatase during fasting and refeeding.