Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

5.4.2.7: phosphopentomutase

This is an abbreviated version!
For detailed information about phosphopentomutase, go to the full flat file.

Word Map on EC 5.4.2.7

Reaction

alpha-D-ribose 1-phosphate
=
D-ribose 5-phosphate

Synonyms

alpha-D-Glucose-1,6-bisphosphate:deoxy-D-ribose-1-phosphate phosphotransferase, alpha-D-ribose1,5-phosphomutase, deoB, Deoxyribomutase, Deoxyribose phosphomutase, EC 2.7.5.6, PGM3, Phosphodeoxyribomutase, Phosphomutase, deoxyribose, phosphopentomutase, Phosphoribomutase, PPM, PPMase

ECTree

     5 Isomerases
         5.4 Intramolecular transferases
             5.4.2 Phosphotransferases (phosphomutases)
                5.4.2.7 phosphopentomutase

Engineering

Engineering on EC 5.4.2.7 - phosphopentomutase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D156A
site-directed mutagenesis, the D156A variant displays a dramatically reduced level of phosphorylation of the active site Thr85 compared to the wild-type, and does not acquire phosphatase activity
K240A
site-directed mutagenesis, the K240A variant can be phosphorylated by the small molecule activator glucose 1,6-bisphosphate like the wild-type enzyme
T85E
site-directed mutagenesis, the T85E variant mimics the active site charge of the activated state of the enzyme, the affinity for activator glucose 1,6-bisphosphate is 4.5fold reduced compared to the wild-type enzyme
T85Q
site-directed mutagenesis, the T85Q variant mimics the active site charge of the unactivated state of the enzyme, the affinity for activator glucose 1,6-bisphosphate is only slightly reduced compared to the wild-type enzyme
D156A
-
site-directed mutagenesis, the D156A variant displays a dramatically reduced level of phosphorylation of the active site Thr85 compared to the wild-type, and does not acquire phosphatase activity
-
K240A
-
site-directed mutagenesis, the K240A variant can be phosphorylated by the small molecule activator glucose 1,6-bisphosphate like the wild-type enzyme
-
T85E
-
site-directed mutagenesis, the T85E variant mimics the active site charge of the activated state of the enzyme, the affinity for activator glucose 1,6-bisphosphate is 4.5fold reduced compared to the wild-type enzyme
-
T85Q
-
site-directed mutagenesis, the T85Q variant mimics the active site charge of the unactivated state of the enzyme, the affinity for activator glucose 1,6-bisphosphate is only slightly reduced compared to the wild-type enzyme
-