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3.9.1.3: phosphohistidine phosphatase

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

Word Map on EC 3.9.1.3

Reaction

a [protein]-N-phospho-L-histidine
+
H2O
=
a [protein]-L-histidine
+
phosphate

Synonyms

14 kDa phosphohistidine phosphatase, 14-kDa phosphohistidine phosphatase, 16 kDa protein histidine phosphatase, histidine protein phosphatase, LHPP, PGAM5, phospho-histidine phosphatase, phosphohistidine phosphatase, phosphohistidine phosphatase 1, phosphohistidine phosphatase I, phosphopolyhistidine phosphatase, PHP, PHP14, PHPT-1, PHPT1, PHPTI, PP1, PP2A, protein histidine phosphatase, protein histidine phosphatase 1, protein-histidine phosphatase, SixA

ECTree

     3 Hydrolases
         3.9 Acting on phosphorus-nitrogen bonds
             3.9.1 Acting on phosphorus-nitrogen bonds (only sub-subclass identified to date)
                3.9.1.3 phosphohistidine phosphatase

Engineering

Engineering on EC 3.9.1.3 - phosphohistidine phosphatase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C69A
-
the mutation does not affect enzyme activity
C69A/C71A
-
the mutations do not affect enzyme activity
C69A/C71A/C73A
-
the mutations do not affect enzyme activity
C69A/C73A
-
the mutation s do not affect enzyme activity
C71A
-
the mutation does not affect enzyme activity
C71A/C73A
-
the mutations do not affect enzyme activity
C73A
-
the mutation does not affect enzyme activity
G75A
-
inacvtive
G75A/G77A/S80A
-
inactive
G77A
-
inacvtive
H102A
inactive
H81A
the mutant shows wild type activity
R45A
the specific activity of the mutant is decreased by one order of magnitude compared to the wild type enzyme
R78A
the specific activity of the mutant is decreased by about 30% compared to the wild type enzyme
H105A
the mutant enzyme shows no dephosphorylation of nucleoside diphosphate kinase B
H53A
-
inactive
additional information
-
deletion of 9 N-terminal amino acids results in inactive enzyme, while 4 C-terminal residues can be deleted without losing enzyme activity