The kinase activity of human brain 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase is regulated via inhibition by phosphoenolpyruvate
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference87 articles.
1. 6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase: suiting structure to need, in a family of tissue-specific enzymes
2. PFK-2/FBPase-2: maker and breaker of the essential biofactor fructose-2,6-bisphosphate
3. 6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis
4. The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies
5. Cloning of cDNA Encoding for a Novel Isozyme of Fructose 6-Phosphate,2-Kinase/Fructose 2,6-Bisphosphatase from Human Placenta
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1. PFK2/FBPase-2 is a potential target for metabolic engineering in the filamentous fungus Myceliophthora thermophila;Frontiers in Microbiology;2022-11-21
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3. The role of PFKFB3 in maintaining colorectal cancer cell proliferation and stemness;Molecular Biology Reports;2022-05-12
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