Menu
Home
People
Places
Arts
History
Plants & Animals
Science
Life & Culture
Technology
Reference.org
Legumin
open-in-new
<h2 id="properties">Properties</h2> <h3>Structure</h3> <p>Legumin is a conjugated protein with six subunits. The individual subunits have a hydrophilic α chain that is initially linked to the smaller hydrophobic β chain with a peptide bond. Both the α and β chains are encoded by the same gene. Each of the six subunits has a mass of ~50-60 kDa. During <a href="/facts/Translation_(biology)/JcPC1rth">translation</a> of the α and β chains, the polypeptide is inserted into the <a href="/facts/Endoplasmic_reticulum/DVbLA7GE">endoplasmic reticulum</a> (ER) where the <a href="/facts/Signal_peptide/9oARjq52">signal peptide</a> that initiated the cell to translocate the chains is cleaved. A <a href="/facts/Disulfide_bridge/eDx5Xtlg">disulfide bridge</a> is formed between the α and β chains to form prolegumin, a <a href="/facts/Protein_precursor/A1vxb5mN">protein precursor</a>. Three of these subunits come together to form a <a href="/facts/Protein_trimer/hCMCasTN">trimer</a> in the ER. The trimer of prolegumins can be transported to the <a href="/facts/Vacuole/9QjBVb7j">vacuole</a> for further <a href="/facts/Post-translational_modification/KMUayTIc">post-translational modification</a>. In the vacuole, the peptide bond formed between the α and β chains is cleaved now that the disulfide bridge holds the two chains together. The cleavage of the α and β chains within the trimers signals protein maturation where two trimers to come together and form the final hexameric legumin protein.<a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a> </p> <h3>Composition</h3> <p>Although legumin is similar to <a href="/facts/Casein/Udl5k8sx">casein</a> of mammalian milk, it contains less carbon and more nitrogen than true casein. <a href="/facts/Karl_Heinrich_Ritthausen/5It2XdBz">Karl Heinrich Ritthausen</a> found legumin from peas, vetches, lentils, and field beans to contain the elements in the following proportions: carbon, 51.48%; hydrogen, 7.02%; nitrogen, 16.77%; and oxygen, 24.32%. When treated with <a href="/facts/Sulfuric_acid/Wom6fymJ">sulfuric acid</a>, legumin breaks down to <a href="/facts/Leucine/X7YrkvA5">leucine</a>, <a href="/facts/Tyrosine/RJhEgE4C">tyrosine</a>, and <a href="/facts/Glutamic_acid/7oXbNcvu">glutamic</a> and <a href="/facts/Aspartic_acid/9DFSFPa1">aspartic acids</a>.<a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a> </p><p>Legumin proteins are relevant because their composition as a <a href="/facts/Storage_protein/4GA7wmxB">storage protein</a> means they are a highly biologically active source of protein. Legumes like beans, lupins, and peas have great nutritional value for humans. They provide an inexpensive but effective low fat protein source. Although peas are commonly consumed as a source leguminous protein, lupins and soybeans provide a much higher protein content. Legumes are also a rich source of <a href="/facts/Essential_amino_acid/Re9Rxb9I">essential amino acids</a>.<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a> </p> <h3>Solubility</h3> <p>Legumin proteins are insoluble in water because of their hydrophobic units.<a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a> Legumins are soluble in very weak <a href="/facts/Acid/FySU18n1">acids</a> and <a href="/facts/Alkalies/s6NqPGSP">alkalies</a>. This protein is not <a href="/facts/Coagulate/vnfEevM0">coagulated</a> by heat.<a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a> Due to their important storage function legumin proteins and another important storage protein <a href="/facts/Vicilin/3Aa6L5Pg">vicilin</a><a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a> have been found be to the most abundant water and alkali soluble proteins within cottonseed.<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a> </p> <h2 id="see-also">See also</h2> <ul><li><a href="/facts/Edestin/1AgBktBd">Edestin</a>, a legumin protein found in hemp</li> <li><a href="/facts/Prolamin/GnnrRWjL">Prolamin</a>, another group of storage proteins in plants</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>"Legumin" . New International Encyclopedia. Vol. XII. 1905. <a href="https://en.wikisource.org/wiki/The_New_International_Encyclop%C3%A6dia/Legumin" target="_blank">https://en.wikisource.org/wiki/The_New_International_Encyclop%C3%A6dia/Legumin</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>"Search: legumin AND organism:"Pisum sativum (Garden pea) [3888]"". UniProtKB. Retrieved 2022-04-26. <a href="https://www.uniprot.org/uniprot/?query=legumin&fil=organism:%22Pisum+sativum+(Garden+pea)+%5B3888%5D%22&sort=score" target="_blank">https://www.uniprot.org/uniprot/?query=legumin&fil=organism:%22Pisum+sativum+(Garden+pea)+%5B3888%5D%22&sort=score</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>"Legumin" . New International Encyclopedia. Vol. XII. 1905. <a href="https://en.wikisource.org/wiki/The_New_International_Encyclop%C3%A6dia/Legumin" target="_blank">https://en.wikisource.org/wiki/The_New_International_Encyclop%C3%A6dia/Legumin</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>He, Zhongqi; Mattison, Christopher P.; Zhang, Dunhua; Grimm, Casey C. (2021-04-28). "Vicilin and legumin storage proteins are abundant in water and alkali soluble protein fractions of glandless cottonseed". Scientific Reports. 11 (1): 9209. doi:10.1038/s41598-021-88527-7. ISSN 2045-2322. PMC 8080652. PMID 33911142. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8080652" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8080652</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>Srivastava, L. M (2002). Plant growth and development: hormones and environment. Amsterdam; Boston: Academic Press. ISBN 978-0-08-051403-1. OCLC 298794614. <a href="978-0-08-051403-1" target="_blank">978-0-08-051403-1</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li> <li id="fn:6"><p>"Legumin" . New International Encyclopedia. Vol. XII. 1905. <a href="https://en.wikisource.org/wiki/The_New_International_Encyclop%C3%A6dia/Legumin" target="_blank">https://en.wikisource.org/wiki/The_New_International_Encyclop%C3%A6dia/Legumin</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li> <li id="fn:7"><p>Maphosa, Yvonne; Jideani, Victoria A. (2017-08-02), Hueda, Maria Chavarri (ed.), "The Role of Legumes in Human Nutrition", Functional Food - Improve Health through Adequate Food, InTech, doi:10.5772/intechopen.69127, ISBN 978-953-51-3439-8, retrieved 2022-05-17 <a href="978-953-51-3439-8" target="_blank">978-953-51-3439-8</a> <a href="#fnref:7" class="footnote-back-ref">↩</a></p></li> <li id="fn:8"><p>Srivastava, L. M (2002). Plant growth and development: hormones and environment. Amsterdam; Boston: Academic Press. ISBN 978-0-08-051403-1. OCLC 298794614. <a href="978-0-08-051403-1" target="_blank">978-0-08-051403-1</a> <a href="#fnref:8" class="footnote-back-ref">↩</a></p></li> <li id="fn:9"><p>"Legumin" . New International Encyclopedia. Vol. XII. 1905. <a href="https://en.wikisource.org/wiki/The_New_International_Encyclop%C3%A6dia/Legumin" target="_blank">https://en.wikisource.org/wiki/The_New_International_Encyclop%C3%A6dia/Legumin</a> <a href="#fnref:9" class="footnote-back-ref">↩</a></p></li> <li id="fn:10"><p>Shutov, A. D.; Kakhovskaya, I. A.; Braun, H.; Bäumlein, H.; Müntz, K. (December 1995). "Legumin-like and vicilin-like seed storage proteins: evidence for a common single-domain ancestral gene". Journal of Molecular Evolution. 41 (6): 1057–1069. doi:10.1007/BF00173187. ISSN 0022-2844. PMID 8587104. S2CID 23465450. <a href="https://pubmed.ncbi.nlm.nih.gov/8587104/#:~:text=Legumin-like%2011S%20and%20vicilin,-terminal%20basic%20beta-chain." target="_blank">https://pubmed.ncbi.nlm.nih.gov/8587104/#:~:text=Legumin-like%2011S%20and%20vicilin,-terminal%20basic%20beta-chain.</a> <a href="#fnref:10" class="footnote-back-ref">↩</a></p></li> <li id="fn:11"><p>He, Zhongqi; Mattison, Christopher P.; Zhang, Dunhua; Grimm, Casey C. (2021-04-28). "Vicilin and legumin storage proteins are abundant in water and alkali soluble protein fractions of glandless cottonseed". Scientific Reports. 11 (1): 9209. doi:10.1038/s41598-021-88527-7. ISSN 2045-2322. PMC 8080652. PMID 33911142. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8080652" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8080652</a> <a href="#fnref:11" class="footnote-back-ref">↩</a></p></li> </ol>