Pseudophosphatases

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List of pseudophosphatases

HP fold

HP1 family

PFKFB subfamily

PFKFB has two enzymatic domains: 6-phosphofructo-2-kinase domain and fructose-2,6-bisphosphatase domain.

  • Human PFKFB3 has low bisphosphatase activity, which is probably due to the R to S substitution at R motif [1, 2].
  • Yeast PFK26 is inactive as indicated by the fructose-2,6-bisphosphatase moiety [3], which probably due to H to S substitution at RH motif.
  • Yeast YLR345W is predicted to be inactive, since the substitution of H by C at RH motif is observed.
STS subfamily

C. elegans has an expansion in STS subfamily. It has five members, however, none of them has SH3 or UBA domain that are common among STSs. We observed substitutions in three STSs from RH..R..Hx to RC..A..Ds, --..K..Dn, RS..R..Ha, respectively.


Note: old version Pseudophosphatases (obsolete)

References

  1. Manes NP and El-Maghrabi MR. The kinase activity of human brain 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase is regulated via inhibition by phosphoenolpyruvate. Arch Biochem Biophys. 2005 Jun 15;438(2):125-36. DOI:10.1016/j.abb.2005.04.011 | PubMed ID:15896703 | HubMed [Manes05]
  2. Cavalier MC, Kim SG, Neau D, and Lee YH. Molecular basis of the fructose-2,6-bisphosphatase reaction of PFKFB3: transition state and the C-terminal function. Proteins. 2012 Apr;80(4):1143-53. DOI:10.1002/prot.24015 | PubMed ID:22275052 | HubMed [Cavalier12]
  3. Kretschmer M, Langer C, and Prinz W. Mutation of monofunctional 6-phosphofructo-2-kinase in yeast to bifunctional 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase. Biochemistry. 1993 Oct 19;32(41):11143-8. PubMed ID:8218176 | HubMed [Kretschmer93]
All Medline abstracts: PubMed | HubMed