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  2. Lactase persistence - Wikipedia

    en.wikipedia.org/wiki/Lactase_persistence

    When these enzymes are produced in low quantities, lactase non-persistence (LNP) results. [38] The ability to digest fresh milk through adulthood is genetically coded for by different variants which are located upstream of the LCT gene and which differ among populations. Those variants are found at very high frequencies in some populations and ...

  3. Lactose intolerance - Wikipedia

    en.wikipedia.org/wiki/Lactose_intolerance

    However, most people worldwide remain lactase non-persistent. [9] Populations that raised animals not used for milk tend to have 90–100 percent of a lactose intolerant rate. [80] For this reason, lactase persistence is of some interest to the fields of anthropology, human genetics, and archaeology, which typically use the genetically derived ...

  4. Inborn errors of carbohydrate metabolism - Wikipedia

    en.wikipedia.org/wiki/Inborn_errors_of...

    However, 5% to 90% of the human population possess an advantageous autosomal mutation in which lactase production persists after infancy. The geographic distribution of lactase persistence is concordant with areas of high milk intake. Lactase non-persistence is common in tropical and subtropical countries.

  5. Lactase - Wikipedia

    en.wikipedia.org/wiki/Lactase

    Mutations are believed to interfere with the function of lactase, causing affected infants to have a severely impaired ability to digest lactose in breast milk or formula. [ 24 ] Some population segments exhibit lactase persistence resulting from a mutation that is postulated to have occurred 5,000–10,000 years ago, coinciding with the rise ...

  6. β-Galactosidase - Wikipedia

    en.wikipedia.org/wiki/Β-Galactosidase

    After a time, certain colonies began to grow. However, the EbgA protein is an ineffective lactase and does not allow growth on lactose. Two classes of single point mutations dramatically improve the activity of ebg enzyme toward lactose. [24] [25] and, as a result, the mutant enzyme is able to replace the lacZ β-galactosidase. [26]

  7. Lactose synthase - Wikipedia

    en.wikipedia.org/wiki/Lactose_synthase

    This causes a conformational change in the large loop which then creates sites for oligosaccharide and metal ion binding, and protein-protein interactions for alpha-lactalbumin. [4] It is important to maintain a sequential order for these binding events to occur, meaning the conformational change needs to occur after the binding of the substrate.

  8. Repressor - Wikipedia

    en.wikipedia.org/wiki/Repressor

    Eventually, the lactase will digest all of the lactose, until there is none to bind to the repressor. The repressor will then bind to the operator, stopping the manufacture of lactase. In molecular genetics, a repressor is a DNA-or RNA-binding protein that inhibits the expression of one or more genes by binding to the operator or associated ...

  9. Lactose permease - Wikipedia

    en.wikipedia.org/wiki/Lactose_permease

    The protein has twelve transmembrane alpha-helices and its molecular weight is 45,000 daltons. [2] It exhibits an internal two-fold symmetry, relating the N-terminal six helices onto the C-terminal helices. It is encoded by the lacY gene in the lac operon. The LacY gene is a component of the lac operon that encodes lactose permease, a protein ...