Alpha-lactalbuminalpha-lactalbumin supplement, alpha-lactalbumin rich foods
4L41, 1A4V, 1B9O, 1CB3, 1HML, 3B0I, 3B0O
|Gene location Human|
|Chr||Chromosome 12 human|
|Gene location Mouse|
|Chr||Chromosome 15 mouse|
|Band||15|15 F1||Start||98,480,400 bp|
|RNA expression pattern|
|More reference expression data|
|Molecular function|| calcium ion binding|
metal ion binding
lactose synthase activity
|Cellular component|| extracellular region|
|Biological process|| apoptotic process|
defense response to bacterium
lactose biosynthetic process
cell wall macromolecule catabolic process
defense response to Gram-negative bacterium
defense response to Gram-positive bacterium
|Sources:Amigo / QuickGO|
α-Lactalbumin is a protein that regulates the production of lactose in the milk of almost all mammalian species In primates, alpha-lactalbumin expression is upregulated in response to the hormone prolactin and increases the production of lactose
α-Lactalbumin forms the regulatory subunit of the lactose synthase LS heterodimer and β-1,4-galactosyltransferase beta4Gal-T1 forms the catalytic component Together, these proteins enable LS to produce lactose by transferring galactose moieties to glucose As a multimer, alpha-lactalbumin strongly binds calcium and zinc ions and may possess bactericidal or antitumor activity A folding variant of human alpha-lactalbumin that may form in acidic environments such as the stomach, called HAMLET, probably induces apoptosis in tumor and immature cells The corresponding folding dynamics of alpha-lactalbumin is thus highly unusual
When formed into a complex with Gal-T1, a galactosyltransferase, α-lactalbumin, enhances the enzyme's affinity for glucose by about 1000 times, and inhibits the ability to polymerise multiple galactose units This gives rise to a pathway for forming lactose by converting Gal-TI to Lactose synthase
The structure of alpha-lactalbumin is well known and is composed of 123 amino acids and 4 disulfide bridges The molecular weight is 14178 Da, and the isoelectric point is between 42 and 45 One of the main structural differences with beta-lactoglobulin is that it does not have any free thiol group that can serve as the starting-point for a covalent aggregation reaction As a result, pure α-lactalbumin will not form gels upon denaturation and acidification
The sequence comparison of α-lactalbumin shows a strong similarity to that of lysozymes, specifically the Ca2+-binding c-lysozyme So the expected evolutionary history is that gene duplication of the c-lysozyme was followed by mutation This gene predates the last common ancestor of mammals and birds, which probably puts its origin at about 300 Ma
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