Difference between revisions of "Pseudophosphatases"
From PhosphataseWiki
(Mark moved page Pseudophosphatases to Pseudophosphatases (obsolete)) |
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| + | == 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->S substitution at motif 2 <cite> Manes05, Cavalier12 </cite>. | ||
| + | * Yeast PFK26 is inactive as indicated by the fructose-2,6-bisphosphatase moiety <cite>Kretschmer93</cite>. | ||
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| + | |||
| + | Note: old version [[Pseudophosphatases (obsolete)]] | ||
| + | |||
| + | == References == | ||
| + | <biblio> | ||
| + | #Cavalier12 pmid=22275052 | ||
| + | #Manes05 pmid=15896703 | ||
| + | #Kretschmer93 pmid=8218176 | ||
| + | </biblio> | ||
Revision as of 23:33, 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->S substitution at motif 2 [1, 2].
- Yeast PFK26 is inactive as indicated by the fructose-2,6-bisphosphatase moiety [3].
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 |
