BRENDA - Enzyme Database show
show all sequences of 3.7.1.4

Cloning and Expression of a Phloretin Hydrolase Gene from Eubacterium ramulus and Characterization of the Recombinant Enzyme

Schoefer, L.; Braune, A.; Blaut, M.; Appl. Environ. Microbiol. 70, 6131-6137 (2004)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
DNA and amino acid sequence determination and analysis, expression in Escherichia coli DH5alpha; gene phy, encoded in the 2,4-diacetylphloroglucinol operon, library screening, DNA and amino acid sequence determination and analysis, sequence comparisons and promoter sequence determination, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain DH5alpha(pPH3)
-
Inhibitors
Inhibitors
Commentary
Organism
Structure
1-bromopyrrolidine-2,5-dione
3% inhibition at 1 mM
-
3-(4-hydroxyphenyl)propionic acid
i.e. phloretate, 30% product inhibition at 0.12 mM; product inhibition
-
Cu2+
15% inhibition at 1 mM
-
CuCl2
85% inhibition at 1 mM
-
N-bromosuccinimide
97% inhibition at 1 mM
-
N-ethylmaleimide
65% inhibition at 1 mM
-
NEM
35% inhibition at 1 mM
-
o-phenanthroline
20% inhibition at 1 mM
-
phloroglucinol
46% product inhibition at 0.12 mM; product inhibition
-
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.013
-
phloretin
pH 7.0, 37°C; recombinant enzyme, pH 7.0, 37°C
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
no affected by Mg2+ and Ca2+; possibly a metal-dependent enzyme, no effects by Ca2+ or Mg2+ on the enzyme activity
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
30000
-
2 * 30846, sequence calculation, 2 * 30000, recombinant enzyme, SDS-PAGE
-
30846
-
2 * 30846, sequence calculation, 2 * 30000, recombinant enzyme, SDS-PAGE
-
55000
-
gel filtration; recombinant enzyme, gel filtration
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
phloretin + H2O
-
-
phloretate + phloroglucinol
-
-
?
phloretin + H2O
-
during flavonoid degradation
phloroglucinol + 3-(4-hydroxyphenyl)propionic acid
-
-
?
phloretin + H2O
wK1
-
phloretate + phloroglucinol
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
-
Q715L4
; gene phy
-
wK1
Q715L4
; gene phy
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme 13.2fold from Escherichia coli strain DH5alpha(pPH3) by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, followed by gel filtration; recombinant enzyme from Escherichia coli, about 13.2fold
-
Reaction
Reaction
Commentary
Organism
phloretin + H2O = phloretate + phloroglucinol
also hydrolyses other C-acetylated phenols related to phloretin
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.0064
-
cell extract
-
8.7
-
purified enzyme; purified recombinant enzyme, pH 7.0, 37°C
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
no activity with phloretin-2'-glucoside, i.e. phloridzin, neohesperidin dihydrochalcone, 1,3-diphenyl-1,3-propandione, and trans-1,3-diphenyl-2,3-epoxy-propan-1-one
654284
-
?
-
-
-
-
additional information
no activity with glycosides phloretin-2'-glucoside (phloridzin) and neohesperidin dihydrochalcone, nor with compounds showing a structure similar to phloretin, such as 1,3-diphenyl-1,3-propandione and trans-1,3-diphenyl-2,3-epoxy-propan-1-one
654284
-
?
-
-
-
-
additional information
no activity with phloretin-2'-glucoside, i.e. phloridzin, neohesperidin dihydrochalcone, 1,3-diphenyl-1,3-propandione, and trans-1,3-diphenyl-2,3-epoxy-propan-1-one
654284
wK1
?
-
-
-
-
additional information
no activity with glycosides phloretin-2'-glucoside (phloridzin) and neohesperidin dihydrochalcone, nor with compounds showing a structure similar to phloretin, such as 1,3-diphenyl-1,3-propandione and trans-1,3-diphenyl-2,3-epoxy-propan-1-one
654284
wK1
?
-
-
-
-
phloretin + H2O
-
654284
-
phloretate + phloroglucinol
-
-
-
?
phloretin + H2O
a C-C bond cleaving enzyme
654284
-
phloretate + phloroglucinol
-
-
-
?
phloretin + H2O
-
654284
wK1
phloretate + phloroglucinol
-
-
-
?
phloretin + H2O
a C-C bond cleaving enzyme
654284
wK1
phloretate + phloroglucinol
-
-
-
?
phloretin + H2O
-
654284
-
phloroglucinol + 3-(4-hydroxyphenyl)propionic acid
-
-
-
ir
phloretin + H2O
during flavonoid degradation
654284
-
phloroglucinol + 3-(4-hydroxyphenyl)propionic acid
-
-
-
?
phloretin + H2O
-
654284
wK1
phloroglucinol + 3-(4-hydroxyphenyl)propionic acid
-
-
-
ir
Subunits
Subunits
Commentary
Organism
dimer
2 * 30000-31000, SDS-PAGE
-
homodimer
2 * 30846, sequence calculation, 2 * 30000, recombinant enzyme, SDS-PAGE
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
10
-
phloretin
pH 7.0, 37°C; recombinant enzyme, pH 7.0, 37°C
-
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
DNA and amino acid sequence determination and analysis, expression in Escherichia coli DH5alpha; gene phy, encoded in the 2,4-diacetylphloroglucinol operon, library screening, DNA and amino acid sequence determination and analysis, sequence comparisons and promoter sequence determination, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain DH5alpha(pPH3)
-
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
1-bromopyrrolidine-2,5-dione
3% inhibition at 1 mM
-
3-(4-hydroxyphenyl)propionic acid
i.e. phloretate, 30% product inhibition at 0.12 mM; product inhibition
-
Cu2+
15% inhibition at 1 mM
-
CuCl2
85% inhibition at 1 mM
-
N-bromosuccinimide
97% inhibition at 1 mM
-
N-ethylmaleimide
65% inhibition at 1 mM
-
NEM
35% inhibition at 1 mM
-
o-phenanthroline
20% inhibition at 1 mM
-
phloroglucinol
46% product inhibition at 0.12 mM; product inhibition
-
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.013
-
phloretin
pH 7.0, 37°C; recombinant enzyme, pH 7.0, 37°C
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
no affected by Mg2+ and Ca2+; possibly a metal-dependent enzyme, no effects by Ca2+ or Mg2+ on the enzyme activity
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
30000
-
2 * 30846, sequence calculation, 2 * 30000, recombinant enzyme, SDS-PAGE
-
30846
-
2 * 30846, sequence calculation, 2 * 30000, recombinant enzyme, SDS-PAGE
-
55000
-
gel filtration; recombinant enzyme, gel filtration
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
phloretin + H2O
-
-
phloretate + phloroglucinol
-
-
?
phloretin + H2O
-
during flavonoid degradation
phloroglucinol + 3-(4-hydroxyphenyl)propionic acid
-
-
?
phloretin + H2O
wK1
-
phloretate + phloroglucinol
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme 13.2fold from Escherichia coli strain DH5alpha(pPH3) by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, followed by gel filtration; recombinant enzyme from Escherichia coli, about 13.2fold
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.0064
-
cell extract
-
8.7
-
purified enzyme; purified recombinant enzyme, pH 7.0, 37°C
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
no activity with phloretin-2'-glucoside, i.e. phloridzin, neohesperidin dihydrochalcone, 1,3-diphenyl-1,3-propandione, and trans-1,3-diphenyl-2,3-epoxy-propan-1-one
654284
-
?
-
-
-
-
additional information
no activity with glycosides phloretin-2'-glucoside (phloridzin) and neohesperidin dihydrochalcone, nor with compounds showing a structure similar to phloretin, such as 1,3-diphenyl-1,3-propandione and trans-1,3-diphenyl-2,3-epoxy-propan-1-one
654284
-
?
-
-
-
-
additional information
no activity with phloretin-2'-glucoside, i.e. phloridzin, neohesperidin dihydrochalcone, 1,3-diphenyl-1,3-propandione, and trans-1,3-diphenyl-2,3-epoxy-propan-1-one
654284
wK1
?
-
-
-
-
additional information
no activity with glycosides phloretin-2'-glucoside (phloridzin) and neohesperidin dihydrochalcone, nor with compounds showing a structure similar to phloretin, such as 1,3-diphenyl-1,3-propandione and trans-1,3-diphenyl-2,3-epoxy-propan-1-one
654284
wK1
?
-
-
-
-
phloretin + H2O
-
654284
-
phloretate + phloroglucinol
-
-
-
?
phloretin + H2O
a C-C bond cleaving enzyme
654284
-
phloretate + phloroglucinol
-
-
-
?
phloretin + H2O
-
654284
wK1
phloretate + phloroglucinol
-
-
-
?
phloretin + H2O
a C-C bond cleaving enzyme
654284
wK1
phloretate + phloroglucinol
-
-
-
?
phloretin + H2O
-
654284
-
phloroglucinol + 3-(4-hydroxyphenyl)propionic acid
-
-
-
ir
phloretin + H2O
during flavonoid degradation
654284
-
phloroglucinol + 3-(4-hydroxyphenyl)propionic acid
-
-
-
?
phloretin + H2O
-
654284
wK1
phloroglucinol + 3-(4-hydroxyphenyl)propionic acid
-
-
-
ir
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 30000-31000, SDS-PAGE
-
homodimer
2 * 30846, sequence calculation, 2 * 30000, recombinant enzyme, SDS-PAGE
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
10
-
phloretin
pH 7.0, 37°C; recombinant enzyme, pH 7.0, 37°C
-
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
-
General Information
General Information
Commentary
Organism
evolution
C-C-cleaving hydrolases catalyzing reactions similar to the reaction carried out by phloretin hydrolase belong to the alpha/beta-hydrolase fold superfamily, but since the phloretin hydrolase sequence of Eubacterium ramulus has no sequence similarity to other C-C-cleaving hydrolases and also does not contain the conserved sequence motif GXSXG, it can be assumed that this enzyme belongs to another enzyme family. The sequences of phloretin hydrolase, Phy, and 2,4-diacetylphloroglucinol hydrolase, PhlG, show no similarities to any other protein sequences with known functions deposited in database
-
physiological function
phloretin hydrolase catalyzes the hydrolytic C-C cleavage of phloretin to phloroglucinol and 3-(4-hydroxyphenyl) propionic acid during flavonoid degradation in Eubacterium ramulus
-
General Information (protein specific)
General Information
Commentary
Organism
evolution
C-C-cleaving hydrolases catalyzing reactions similar to the reaction carried out by phloretin hydrolase belong to the alpha/beta-hydrolase fold superfamily, but since the phloretin hydrolase sequence of Eubacterium ramulus has no sequence similarity to other C-C-cleaving hydrolases and also does not contain the conserved sequence motif GXSXG, it can be assumed that this enzyme belongs to another enzyme family. The sequences of phloretin hydrolase, Phy, and 2,4-diacetylphloroglucinol hydrolase, PhlG, show no similarities to any other protein sequences with known functions deposited in database
-
physiological function
phloretin hydrolase catalyzes the hydrolytic C-C cleavage of phloretin to phloroglucinol and 3-(4-hydroxyphenyl) propionic acid during flavonoid degradation in Eubacterium ramulus
-
Other publictions for EC 3.7.1.4
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
750528
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1
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13
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1
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1
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1
1
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1
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2
2
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752294
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1
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1
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1
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1
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1
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1
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1
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1
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1
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1
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2
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1
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685892
Bulhoes
Correlation between lactose ab ...
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40
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-
1
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1
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1
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1
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1
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2
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1
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1
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1
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1
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2
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687838
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Genotyping of the lactase-phlo ...
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12
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-
1
-
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1
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-
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1
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1
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1
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2
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1
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1
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1
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1
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2
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673123
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Genotyping of the lactase-phlo ...
Homo sapiens
Clin. Chem.
52
148-151
2006
-
1
-
-
1
-
-
-
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1
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1
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1
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3
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1
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1
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1
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1
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3
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675574
Kuranuki
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1
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