" /> Lactase-Phlorizin hydrolase - CISMeF





Preferred Label : Lactase-Phlorizin hydrolase;

MeSH definition : The multifunctional protein that contains two enzyme domains. The first domain (EC 3.2.1.62) hydrolyzes glycosyl-N-acylsphingosine to a sugar and N-acylsphingosine. The second domain (EC 3.2.1.108) hydrolyzes LACTOSE and is found in the intestinal brush border membrane. Loss of activity for this enzyme in humans results in LACTOSE INTOLERANCE.; A multifunctional protein that contains two enzyme domains. The first domain (EC 3.2.1.62) hydrolyzes glycosyl-N-acylsphingosine to a sugar and N-acylsphingosine. The second domain (EC 3.2.1.108) hydrolyzes LACTOSE and is found in the intestinal brush border membrane. Loss of activity for this enzyme in humans results in LACTOSE INTOLERANCE.;

MeSH synonym : hydrolase, Lactase-Phlorizin; lactase phlorizin hydrolase; Lactase-Glycosylceramidase; lactase glycosylceramidase;

CISMeF synonym : Glucosyl-N-acylsphingosine glycohydrolase; glycosyl ceramidase; phloretin-glucosidase; phlorizin hydrolase;

MeSH hyponym : Hydrolase, Phlorizin;

Related MeSH term : Phloretin Glucosidase; Ceramidase, Glycosyl; Glycosylceramidase;

MeSH Related Number : EC 3.2.1.108;

Registry Number MeSH : EC 3.2.1.62;

Wikipedia link : https://en.wikipedia.org/wiki/Glycosylceramidase;

Is substance : O;

UNII : EC 3.2.1.62;

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The multifunctional protein that contains two enzyme domains. The first domain (EC 3.2.1.62) hydrolyzes glycosyl-N-acylsphingosine to a sugar and N-acylsphingosine. The second domain (EC 3.2.1.108) hydrolyzes LACTOSE and is found in the intestinal brush border membrane. Loss of activity for this enzyme in humans results in LACTOSE INTOLERANCE.
A multifunctional protein that contains two enzyme domains. The first domain (EC 3.2.1.62) hydrolyzes glycosyl-N-acylsphingosine to a sugar and N-acylsphingosine. The second domain (EC 3.2.1.108) hydrolyzes LACTOSE and is found in the intestinal brush border membrane. Loss of activity for this enzyme in humans results in LACTOSE INTOLERANCE.

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28/04/2025


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