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3.7.1.4: phloretin hydrolase

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

Word Map on EC 3.7.1.4

Reaction

phloretin
+
H2O
=
phloretate
+
phloroglucinol

Synonyms

C-acylphenol acylhydrolase, lactase phlorizin hydrolase, lactase phlorizin-hydrolase, lactase-phlorizin hydrolase, lactase/phlorizin hydrolase, LCT, LPH, Phlg, phloretin hydrolase, Phy, PNG hydrolase

ECTree

     3 Hydrolases
         3.7 Acting on carbon-carbon bonds
             3.7.1 In ketonic substances
                3.7.1.4 phloretin hydrolase

Engineering

Engineering on EC 3.7.1.4 - phloretin hydrolase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A126S
site-directed mutagenesis
F218Y
site-directed mutagenesis
N1340Q
-
the variant lacks the closest potential N-glycosylation site to Asp1338
N1814Q
-
the variant lacks the N-glycosylation site in the domain IV
N821Q
-
the variant lacks the N-glycosylation site in the domain II
A213S
-
the mutant completely loses catalytic activity towards phloretin
E164A
-
the mutation completely abolishes the hydrolytic activity towards phloretin
E273A
-
the mutation completely abolishes the hydrolytic activity towards phloretin
H118A
-
the mutant completely loses catalytic activity towards phloretin
H133A
-
the kcat value for phloretin is decreased at least by 1 order of magnitude, whereas the corresponding Km value is barely affected compared to the wild type enzyme
H160A
-
the mutant completely loses catalytic activity towards phloretin
H160F
-
the mutant completely loses catalytic activity towards phloretin
H217A
-
the mutant has a Km value increased by 3fold and a kcat value decreased by 6fold compared to the wild type enzyme
H269A
-
the kcat value for phloretin is decreased at least by 1 order of magnitude, whereas the corresponding Km value is barely affected compared to the wild type enzyme
I162A
-
the mutant completely loses catalytic activity towards phloretin
Q266F
-
the mutant completely loses catalytic activity towards phloretin
Y125A
-
the mutant completely loses catalytic activity towards phloretin
Y232A
-
the Km value for phloretin increases by 3fold and the kcat value decreases by 5fold compared to the wild type enzyme
E164A
-
the mutation completely abolishes the hydrolytic activity towards phloretin
-
E273A
-
the mutation completely abolishes the hydrolytic activity towards phloretin
-
H118A
-
the mutant completely loses catalytic activity towards phloretin
-
H160A
-
the mutant completely loses catalytic activity towards phloretin
-
H160F
-
the mutant completely loses catalytic activity towards phloretin
-
additional information