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1BIF

6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE BIFUNCTIONAL ENZYME COMPLEXED WITH ATP-G-S AND PHOSPHATE

Summary for 1BIF
Entry DOI10.2210/pdb1bif/pdb
NMR InformationBMRB: 5935
Descriptor6-PHOSPHOFRUCTO-2-KINASE/ FRUCTOSE-2,6-BISPHOSPHATASE, MAGNESIUM ION, PHOSPHATE ION, ... (6 entities in total)
Functional Keywordskinase, transferase (phospho), phosphatase, hydrolase (phospho), glycolysis, bifunctional enzyme
Biological sourceRattus norvegicus (Norway rat)
Total number of polymer chains1
Total formula weight54898.17
Authors
Hasemann, C.A.,Deisenhofer, J. (deposition date: 1996-11-08, release date: 1997-11-12, Last modification date: 2024-02-07)
Primary citationHasemann, C.A.,Istvan, E.S.,Uyeda, K.,Deisenhofer, J.
The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies.
Structure, 4:1017-1029, 1996
Cited by
PubMed Abstract: Glucose homeostasis is maintained by the processes of glycolysis and gluconeogenesis. The importance of these pathways is demonstrated by the severe and life threatening effects observed in various forms of diabetes. The bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase catalyzes both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis. Thus this bifunctional enzyme plays an indirect yet key role in the regulation of glucose metabolism.
PubMed: 8805587
DOI: 10.1016/S0969-2126(96)00109-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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