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

BRENDA support

3.6.1.25: triphosphatase

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

Word Map on EC 3.6.1.25

Reaction

Triphosphate
+
H2O
=
diphosphate
+
phosphate

Synonyms

inorganic triphosphatase, triphosphate tunnel metalloenzyme, tripolyphosphatase, TTM

ECTree

     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.25 triphosphatase

Engineering

Engineering on EC 3.6.1.25 - triphosphatase

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
K52R
-
the His-tagged mutant loses 90-99% of its activity (catalytic efficiency is at least 1000times lower) compared to the wild type enzyme. Mn2+ does not induce a significant activation of this mutant
K85A
-
the His-tagged mutant is about 10times less active than the wild type enzyme, but the optimal conditions for activity are essentially the same. The mutant is more strongly activated by Mn2+ than by Mg2+, and the inhibitory effects of Ca2+ and Zn2+ are less pronounced
K8A
-
the His-tagged mutant remains highly active with tripolyphosphate as substrate and Mg2+ as activator, with a catalytic efficiency close to that of the recombinant wild type enzyme
R265H
-
no AdoMet synthetase activity, normal tripolyphosphatase activity
R265S
-
no AdoMet synthetase activity, reduced tripolyphosphatase activity