(Q38335879)

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Directed mutations in the poorly defined region of porcine liver fructose-1,6-bisphosphatase significantly affect catalysis and the mechanism of AMP inhibition

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scholarly article

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Europe PubMed Central

2 September 2017

Directed mutations in the poorly defined region of porcine liver fructose-1,6-bisphosphatase significantly affect catalysis and the mechanism of AMP inhibition (English)

1 reference

Europe PubMed Central

2 September 2017

author name string

Kurbanov FT

1

1 reference

Europe PubMed Central

2 September 2017

Choe JY

2

1 reference

Europe PubMed Central

2 September 2017

Honzatko RB

3

1 reference

Europe PubMed Central

2 September 2017

Fromm HJ

4

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Europe PubMed Central

2 September 2017

language of work or name

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publication date

1 July 1998

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Europe PubMed Central

2 September 2017

Journal of Biological Chemistry

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Europe PubMed Central

2 September 2017

273

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Europe PubMed Central

2 September 2017

28

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Europe PubMed Central

2 September 2017

17511-17516

1 reference

Europe PubMed Central

2 September 2017

The Allosteric Properties of Beef-Liver Fructose Bisphosphatase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Inhibition of fructose-1,6-bisphosphatase by fructose 2,6-biphosphate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Hormonal regulation of hepatic gluconeogenesis and glycolysis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Complete amino acid sequence of pig kidney fructose-1,6-bisphosphatase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Structure refinement of fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex at 2.8 A resolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Crystal structure of the neutral form of fructose 1,6-bisphosphatase complexed with regulatory inhibitor fructose 2,6-bisphosphate at 2.6-A resolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Evidence for an active T-state pig kidney fructose 1,6-bisphosphatase: interface residue Lys-42 is important for allosteric inhibition and AMP cooperativity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Site-directed mutagenesis of virtually any plasmid by eliminating a unique site

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

High-level expression of porcine fructose-1,6-bisphosphatase in Escherichia coli: purification and characterization of the enzyme.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

1 reference

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21 January 2018

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

A computer program for fitting and statistically analyzing initial rate data applied to bovine hexokinase type III isozyme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Toward a mechanism for the allosteric transition of pig kidney fructose-1,6-bisphosphatase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Studies on the mechanism of adenosine 5'-monophosphate inhibition of bovine liver fructose 1,6-bisphosphatase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Regulation of rabbit liver fructose-1,6-bisphosphatase by metals, nucleotides, and fructose 2,6-bisphosphate as determined from fluorescence studies

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Biochemical properties of mutant and wild-type fructose-1,6-bisphosphatases are consistent with the coupling of intra- and intersubunit conformational changes in the T- and R-state transition

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Major changes in the kinetic mechanism of AMP inhibition and AMP cooperativity attend the mutation of Arg49 in fructose-1,6-bisphosphatase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Importance of the dimer-dimer interface for allosteric signal transduction and AMP cooperativity of pig kidney fructose-1,6-bisphosphatase. Site-specific mutagenesis studies of Glu-192 and Asp-187 residues on the 190's loop

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Spinach chloroplast fructose-1,6-bisphosphatase: identification of the subtilisin-sensitive region and of conserved histidines

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

60 Fructose-1,6-diphosphatase from rabbit liver

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

On the mechanism of inhibition of fructose 1,6-bisphosphatase by fructose 2,6-bisphosphate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Conservation of primary structure at the proteinase-sensitive site of fructose 1,6-bisphosphatases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Glutamic acid residue 98 is critical for catalysis in pig kidney fructose-1,6-bisphosphatase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Mutation of arginine 276 to methionine changes Mg2+ cooperativity and the kinetic mechanism of fructose-1,6-bisphosphatase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.28.17511

21 January 2018

Identifiers

10.1074/JBC.273.28.17511

1 reference

Europe PubMed Central

2 September 2017

1 reference

Europe PubMed Central

2 September 2017

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