User:Cboursnell/Sandbox/6PF2K

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6PF2K
crystal structure of human liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Identifiers
Symbol6PF2K
PfamPF01591
Pfam clanCL0023
InterProIPR013079
PROSITEPDOC00158
SCOP21bif / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

6-Phosphofructo-2-kinase (EC, EC) is a bifunctional enzyme that catalyses both the synthesis and the degradation of fructose-2, 6-bisphosphate. The fructose-2,6-bisphosphatase reaction involves a phosphohistidine intermediate. The catalytic pathway is:

ATP + D-fructose 6-phosphate = ADP + D-fructose 2,6-bisphosphate

D-fructose 2,6-bisphosphate + H2O = 6-fructose 6-phosphate + Pi

The enzyme is important in the regulation of hepatic carbohydrate metabolism and is found in greatest quantities in the liver, kidney and heart. In mammals, several genes often encode different isoforms, each of which differs in its tissue distribution and enzymatic activity.[1] The family described here bears a resemblance to the ATP-driven phospho-fructokinases, however, they share little sequence similarity, although a few residues seem key to their interaction with fructose 6-phosphate.[2]

This domain forms the N-terminal region of this enzyme, while INTERPRO forms the C-terminal domain.


References[edit]

  1. ^ Heine-Suñer D, DÃaz-Guillén MA, Lange AJ, RodrÃguez de Córdoba S (May 1998). "Sequence and structure of the human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase heart isoform gene (PFKFB2)". Eur. J. Biochem. 254 (1): 103–110. doi:10.1046/j.1432-1327.1998.2540103.x. PMID 9652401.{{cite journal}}: CS1 maint: date and year (link) CS1 maint: multiple names: authors list (link)
  2. ^ Wang X, Deng Z, Kemp RG (September 1998). "An essential methionine residue involved in substrate binding by phosphofructokinases". Biochem. Biophys. Res. Commun. 250 (2): 466–468. doi:10.1006/bbrc.1998.9311. PMID 9753654.{{cite journal}}: CS1 maint: date and year (link) CS1 maint: multiple names: authors list (link)
This article incorporates text from the public domain Pfam and InterPro: IPR013079

Category:Protein domains