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Results 1 - 6 of 6
EC Number
General Information
Commentary
Reference
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
metabolism
the enzyme is involved in the metabolic pathway of icariin, epimedin A, B, and C, and f baohuoside I in intestinal flora and enzyme of rats, detailed overview
more
comparison of the enzyme phloretin hydrolase Phy from Eubacterium ramulus with the diacetyl phloroglucinol hydrolase (Phlg) from Pseudomonas fluorescens, which catalyses a similar, hydrolytic, de-acylation of its substrate, homology modeling of Phy based on the structure of Phlg, PDB ID 3HWP
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
physiological function
the enzyme catalyses the degradation of plant-derived dihydrochalcone phloretin
physiological function
the enzyme plays a major role in the deglycosylation of daidzin
Results 1 - 6 of 6