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.

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 |
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 |
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. DOI:10.1021/bi00092a025 |