Β-Galactosidase: Difference between revisions
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{{Short description|Enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides}} | {{Short description|Enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides}} | ||
'''β-Galactosidase''' (β-gal) is an [[enzyme]] that catalyzes the hydrolysis of [[β-galactosides]] into their constituent [[monosaccharides]]. It is an essential enzyme in carbohydrate metabolism and is commonly found in [[bacteria]], [[fungi]], and [[mammals]]. In humans, a deficiency in β-galactosidase activity is associated with certain [[lysosomal storage disorders]]. | '''β-Galactosidase''' (β-gal) is an [[enzyme]] that catalyzes the hydrolysis of [[β-galactosides]] into their constituent [[monosaccharides]]. It is an essential enzyme in carbohydrate metabolism and is commonly found in [[bacteria]], [[fungi]], and [[mammals]]. In humans, a deficiency in β-galactosidase activity is associated with certain [[lysosomal storage disorders]]. | ||
Latest revision as of 09:17, 14 March 2025
Enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides
β-Galactosidase (β-gal) is an enzyme that catalyzes the hydrolysis of β-galactosides into their constituent monosaccharides. It is an essential enzyme in carbohydrate metabolism and is commonly found in bacteria, fungi, and mammals. In humans, a deficiency in β-galactosidase activity is associated with certain lysosomal storage disorders.
Function[edit]
β-Galactosidase hydrolyzes β-galactosides, breaking the glycosidic bond between a galactose molecule and its linked sugar. This enzyme plays a crucial role in:
- The breakdown of lactose into glucose and galactose.
- The degradation of complex carbohydrates in metabolic pathways.
- Cellular signal transduction in some bacterial systems.
Biochemical Properties[edit]
- Enzyme classification: EC 3.2.1.23
- Substrates: β-galactosides, including lactose.
- Products: Monosaccharides such as glucose and galactose.
- Cofactors: Metal ions like Mg²⁺ may enhance activity.
- Optimal pH: Varies by species, commonly around pH 6–8.
β-Galactosidase in Bacteria[edit]
In Escherichia coli (E. coli), β-galactosidase is encoded by the lacZ gene, part of the lac operon. This enzyme allows E. coli to metabolize lactose when glucose is unavailable.
The lac operon consists of:
- lacZ – Encodes β-galactosidase.
- lacY – Encodes lactose permease, which transports lactose into the cell.
- lacA – Encodes thiogalactoside transacetylase, with an unclear role in lactose metabolism.
β-Galactosidase in E. coli can be measured using X-gal, which produces a blue color when hydrolyzed, a key feature in blue-white screening used in molecular biology.
β-Galactosidase in Humans[edit]
In humans, β-galactosidase is found in the lysosome and is responsible for breaking down glycosphingolipids. Mutations in the GLB1 gene lead to:
- GM1 gangliosidosis – A severe neurodegenerative disorder.
- Mucopolysaccharidosis type IV (Morquio syndrome B) – A metabolic disorder affecting bones and cartilage.
Industrial and Clinical Applications[edit]
β-Galactosidase has various applications in:
- Dairy industry – Used in lactose-free milk production.
- Molecular biology – Utilized in blue-white screening for detecting recombinant plasmids.
- Medical diagnostics – Studied for enzyme replacement therapies in lysosomal storage disorders.
Related Enzymes[edit]
- α-Galactosidase – Hydrolyzes α-galactosides.
- Lactase – Another enzyme involved in lactose digestion.