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α-Galactosidase ( EC 3.2.1.22, α-GAL, α-GAL A; systematic name α-D-galactoside galactohydrolase) is a glycoside hydrolase enzyme that catalyses the following reaction: [1] Hydrolysis of terminal, non-reducing α- D -galactose residues in α- D -galactosides, including galactose oligosaccharides, galactomannans and galactolipids
When the target gene is not found in the vector, the alpha fragment gene would be active, producing the alpha fragment and allowing for B-galactosidase to gain its activity. To trace the activity of B-galactosidase a colorless analog of lactose is used, X-gal. The hydrolysis of X-gal by B-galactosidase produces galactose, a blue colored compound.
However the enzyme can be found in many plants (especially fruits), mammals, yeast, bacteria, and fungi. [29] β-galactosidase genes can differ in the length of their coding sequence and the length of proteins formed by amino acids. [30] This separates the β-galactosidases into four families: GHF-1, GHF-2, GHF-35, and GHF- 42. [31] E.
Raffinose can be hydrolyzed to D-galactose and sucrose by the enzyme α-galactosidase (α-GAL), an enzyme synthesized by bacteria found in the large intestine. α-GAL also hydrolyzes other α-galactosides such as stachyose, verbascose, and galactinol, if present. In plants, raffinose plays a significant role in stress responses, particularly ...
Colonies that produce β-galactosidase are turned blue by X-gal (5-bromo-4-chloro-3-indolyl-β-D-galactoside) which is an artificial substrate for B-galactosidase whose cleavage results in galactose and 4-Cl,3-Br indigo thus producing a deep blue color. [16] Allolactose is an isomer of lactose and is the inducer of the lac operon. Lactose is ...
In prokaryotes, they are found both as intracellular and extracellular enzymes that are largely involved in nutrient acquisition. One of the important occurrences of glycoside hydrolases in bacteria is the enzyme beta-galactosidase (LacZ), which is involved in regulation of expression of the lac operon in E. coli.
The enzyme UDP-glucose 4-epimerase (EC 5.1.3.2), also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. [1]
This enzyme causes bacteria expressing the gene to appear blue when grown on a medium that contains the substrate analog X-gal. An example of a selectable marker which is also a reporter in bacteria is the chloramphenicol acetyltransferase (CAT) gene, which confers resistance to the antibiotic chloramphenicol .