Difference between revisions of "Pseudophosphatases"
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===== PFKFB subfamily ===== | ===== PFKFB subfamily ===== | ||
PFKFB has two enzymatic domains: 6-phosphofructo-2-kinase domain and fructose-2,6-bisphosphatase domain. | 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 | + | * Human PFKFB3 has low bisphosphatase activity, which is probably due to the R to S substitution at R motif <cite> Manes05, Cavalier12 </cite>. |
| − | * Yeast PFK26 is inactive as indicated by the fructose-2,6-bisphosphatase moiety <cite>Kretschmer93</cite>. | + | * Yeast PFK26 is inactive as indicated by the fructose-2,6-bisphosphatase moiety <cite>Kretschmer93</cite>, 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. | ||
Revision as of 23:35, 11 February 2016
The page is under construction.
Contents
List of pseudophosphatases
CC1 fold
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
- 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 |
- 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 |
- 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 |
