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
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3.7.1.4
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eubacterium
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ramulus
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brush
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flavonoid
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border
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medicine
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2,4-diacetylphloroglucinol
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lactase-phlorizin
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molecular biology
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lactase
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pyridoxine
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phloridzin
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flavone
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beta-glucosidic
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carbon-carbon
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beta-glucosidase
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fluorescens
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deglycosylated
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mucosal
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5'-phosphate
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fecal
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dihydrochalcone
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pyridoxal
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abscessus
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neohesperidin
- 3.7.1.4
- eubacterium
- ramulus
-
brush
- flavonoid
- border
- medicine
- 2,4-diacetylphloroglucinol
-
lactase-phlorizin
- molecular biology
- lactase
- pyridoxine
- phloridzin
- flavone
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beta-glucosidic
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carbon-carbon
- beta-glucosidase
- fluorescens
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deglycosylated
- mucosal
- 5'-phosphate
-
fecal
- dihydrochalcone
- pyridoxal
- abscessus
- neohesperidin
Reaction
Synonyms
C-acylphenol acylhydrolase, lactase phlorizin hydrolase, lactase phlorizin-hydrolase, lactase-phlorizin hydrolase, lactase/phlorizin hydrolase, LCT, LPH, Phlg, phloretin hydrolase, Phy, PNG hydrolase
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Engineering
Engineering on EC 3.7.1.4 - phloretin hydrolase
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N1340Q
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the variant lacks the closest potential N-glycosylation site to Asp1338
A213S
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the mutant completely loses catalytic activity towards phloretin
E164A
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the mutation completely abolishes the hydrolytic activity towards phloretin
E273A
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the mutation completely abolishes the hydrolytic activity towards phloretin
H118A
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the mutant completely loses catalytic activity towards phloretin
H133A
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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
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the mutant completely loses catalytic activity towards phloretin
H160F
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the mutant completely loses catalytic activity towards phloretin
H217A
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the mutant has a Km value increased by 3fold and a kcat value decreased by 6fold compared to the wild type enzyme
H269A
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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
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the mutant completely loses catalytic activity towards phloretin
Q266F
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the mutant completely loses catalytic activity towards phloretin
Y125A
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the mutant completely loses catalytic activity towards phloretin
Y232A
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the Km value for phloretin increases by 3fold and the kcat value decreases by 5fold compared to the wild type enzyme
E164A
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the mutation completely abolishes the hydrolytic activity towards phloretin
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E273A
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the mutation completely abolishes the hydrolytic activity towards phloretin
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H118A
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the mutant completely loses catalytic activity towards phloretin
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H160A
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the mutant completely loses catalytic activity towards phloretin
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H160F
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the mutant completely loses catalytic activity towards phloretin
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additional information
mutation of His123, His251, Glu154 and Glu255 (conserved zinc binding residues) results in variants that were either poorly expressed, or of much reduced activity. Mutation of Tyr115 and His203, thought to bind the phenol groups in the 1-and 3-positions of the phloroglucinol ring respectively, results in variants of 15-fold reduced activity and an inactive variant
additional information
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hypolactasia seems to be strongly corretated with genotype C/C of the genetic variant C->T-13910 upstream of the lactase-phlorizin hydrolase gene
additional information
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the genetic variant C/T-13910 upstream of the lactase-phlorizin hydrolase gene is strongly correlated with the lactase persistence/nonperistence trait
additional information
the mutations C/T-13910 and G/A-22018 of the lactase-phlorizin hydrolase gene are correlated with lactose absorption
additional information
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Gata4 mutant, LPH mRNA abundance is significantly attenuated
additional information
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deletions of the LPH 5' flanking sequence and fusion 5' to the human growth hormone reporter gene