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
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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:
