Difference between revisions of "Pseudophosphatases"
From PhosphataseWiki
(Mark moved page Pseudophosphatases to Pseudophosphatases (obsolete)) |
|||
| Line 1: | Line 1: | ||
| − | + | The page is under construction. | |
| + | |||
| + | == 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>. | ||
| + | |||
| + | |||
| + | 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
Error fetching PMID 22275052:
Error fetching PMID 15896703:
Error fetching PMID 8218176:
Error fetching PMID 15896703:
Error fetching PMID 8218176:
- Error fetching PMID 15896703:
- Error fetching PMID 22275052:
- Error fetching PMID 8218176:
