Modification of the ATP inhibitory site of the Ascaris suum phosphofructokinase results in the stabilization of an inactive T state
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00105a026
Reference23 articles.
1. AFFINITY LABELING OF PURINE NUCLEOTIDE SITES IN PROTEINS
2. Correlation between hysteresis and allosteric properties for phosphofructokinase from Ascaris suum.
3. Identification of the chemical groups involved in the binding of periodate-oxidized NADP+ to 6-phosphogluconate dehydrogenase
4. Pyruvate Carboxylase Affinity Labelling of the Magnesium Adenosine Triphosphate Binding Site
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1. Molecular and biochemical characterisation of abomasal nematode parasites Teladorsagia circumcincta and Haemonchus contortus phosphofructokinases and their recognition by the immune host;Experimental Parasitology;2015-04
2. The kinetics and regulation of phosphofructokinase from Teladorsagia circumcincta;Experimental Parasitology;2012-04
3. Optimum Activity of the Phosphofructokinase from Ascaris suum Requires More Than One Metal Ion;Biochemistry;2006-01-28
4. Chemical Modification of SH Groups of E. coli Phosphofructokinase-2 Induces Subunit Dissociation: Monomers Are Inactive but Preserve Ligand Binding Properties;Archives of Biochemistry and Biophysics;2000-04
5. Kinetic Characterization of a T-State ofAscaris suumPhosphofructokinase with Heterotropic Negative Cooperativity by ATP Eliminated;Archives of Biochemistry and Biophysics;1999-05
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