User:Claire Lupton: Difference between revisions

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'''Glutamine Synthetase:'''

<scene name='83/837873/Lengsin/2'>Lengsin</scene> (2J9I), is a protein associated with structural formation of the eye. Lengsin has evolutionary relation to <scene name='83/837873/Human_glutamine_synthetase/1'>Glutamine synthetases</scene>, which gives rise to the term lengsin (LENs Glutamine SYNthetase). This protein is specifically classified as a Glutamine Synthetase I, a part of the Glutamine synthetase superfamily. Glutamine synthetases are most well known for their presence in the urea cycle, where they detoxify nitrogen in the body. In other words, Glutamine Synthetases fixate ammonium and create glutamate mechanistically through the utilization of adenosine triphosphate (ATP) and help make the metabolic processes happen. Despite its close relation to this class of enzymes, lengsin, however, does not have any enzymatic activity, and is, therefore, not necessarily metabolic.<ref name=ref1>PMID:Grassi , F. J., Moretto, N. J., Rivetti, C. J., Cellai, S. J., Betti, M. J., Márquez , A. Ontonello, S. J. (2006). Structural and Functional Properties of Lengsin, a Pseduo-Glutamine Synthetase in the Transparent Human Lens . Retrieved from https://maryville.illiad.oclc.org/illiad/pdf/173917.pdf</ref>

<scene name='83/837873/Lengsin/4'>Lengsin</scene> (2J9I), is a protein associated with structural formation of the eye. Lengsin has evolutionary relation to <scene name='83/837873/Human_glutamine_synthetase/1'>Glutamine synthetases</scene>, which gives rise to the term lengsin (LENs Glutamine SYNthetase). This protein is specifically classified as a Glutamine Synthetase I, a part of the Glutamine synthetase superfamily. Glutamine synthetases are most well known for their presence in the urea cycle, where they detoxify nitrogen in the body. In other words, Glutamine Synthetases fixate ammonium and create glutamate mechanistically through the utilization of adenosine triphosphate (ATP) and help make the metabolic processes happen. Despite its close relation to this class of enzymes, lengsin, however, does not have any enzymatic activity, and is, therefore, not necessarily metabolic.<ref name=ref1>PMID:Grassi , F. J., Moretto, N. J., Rivetti, C. J., Cellai, S. J., Betti, M. J., Márquez , A. Ontonello, S. J. (2006). Structural and Functional Properties of Lengsin, a Pseduo-Glutamine Synthetase in the Transparent Human Lens . Retrieved from https://maryville.illiad.oclc.org/illiad/pdf/173917.pdf</ref>

In fact, no catalytic function was present in multiple assays. lengsin was, therefore, declared a noncatalytic dodecamer. Possible reasons for the lack of activity in lengsin could relate to the binding of NH4+ and ATP to the protein, or its inflexibility when transforming to an oligomeric form. Moreover, this protein was first found in a house mouse (mus muluscus) via electron microscopy, and it has been found to have been an important <scene name='83/837873/Evoluntionary_conservation/1'>evolutionary stepping stone</scene> in the formation of the eye lens in several vertebrate species.<ref name=ref1>PMID:Wyatt, K., White, H. E., Wang, L., Bateman, O. A., Slingsby, C., Orlova, E. V., & Wistow, G. (2006). Lengsin is a survivor of an ancient family of class I glutamine synthetases re-engineered by evolution for a role in the vertebrate lens. Structure (London, England : 1993), 14(12), 1823–1834. https://doi.org/10.1016/j.str.2006.10.008</ref>

Studies have revealed that the evidence for Lengsin’s evolutionary significance lies within the genes which code for this protein. In the N-terminal domain, lies specific exons <ref name=ref2>PMID:Wyatt, K., White, H. E., Wang, L., Bateman, O. A., Slingsby, C., Orlova, E. V., & Wistow, G. (2006). Lengsin is a survivor of an ancient family of class I glutamine synthetases re-engineered by evolution for a role in the vertebrate lens. Structure (London, England : 1993), 14(12), 1823–1834. https://doi.org/10.1016/j.str.2006.10.008</ref>. Through studying the removal and addition of these exons in multiple species, scientists discovered an inactive exon (pseudoexon) in humans which points to clear evolutionary evidence. In many other non-mammalian species, this exon still provides relevance to their overall genome. However, in humans, the pseudoexon is nothing but an extra bit of genetic coding with no known genetic value. For example, comparisons done in fish and birds revealed the activity of multiple exons, including the exon in the n-terminal domain. However, the comparative lengths and numbers of the exons did change within species. <ref name=ref2>PMID:Wyatt, K., White, H. E., Wang, L., Bateman, O. A., Slingsby, C., Orlova, E. V., & Wistow, G. (2006). Lengsin is a survivor of an ancient family of class I glutamine synthetases re-engineered by evolution for a role in the vertebrate lens. Structure (London, England : 1993), 14(12), 1823–1834. https://doi.org/10.1016/j.str.2006.10.008</ref> The most commonly researched Lengsin dependent species are birds, mice, and fish. Research found that lengsin in zebrafish was about 3,000 base pairs, composed of 4 exons, located on chromosome 11 in the zebrafish embryos. In contrast, mammalian lengsin is approximately 5 exons, located on chromosome 6, so it only shares about 40% genetic similarity to mice and human versions of the protein. <ref name=ref1>PMID:Grassi , F. J., Moretto, N. J., Rivetti, C. J., Cellai, S. J., Betti, M. J., Márquez , A. Ontonello, S. J. (2006). Structural and Functional Properties of Lengsin, a Pseduo-Glutamine Synthetase in the Transparent Human Lens . Retrieved from https://maryville.illiad.oclc.org/illiad/pdf/173917.pdf</ref> Nonetheless, this protein performs significant tasks in vertebral species by modifying and creating the structure of the lens as well as executing some other specific functions.

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 '''Glutamine Synthetase:'''
-<scene name='83/837873/Lengsin/2'>Lengsin</scene> (2J9I), is a protein associated with structural formation of the eye. Lengsin has evolutionary relation to <scene name='83/837873/Human_glutamine_synthetase/1'>Glutamine synthetases</scene>, which gives rise to the term lengsin (LENs Glutamine SYNthetase). This protein is specifically classified as a Glutamine Synthetase I, a part of the Glutamine synthetase superfamily. Glutamine synthetases are most well known for their presence in the urea cycle, where they detoxify nitrogen in the body. In other words, Glutamine Synthetases fixate ammonium and create glutamate mechanistically through the utilization of adenosine triphosphate (ATP) and help make the metabolic processes happen. Despite its close relation to this class of enzymes, lengsin, however, does not have any enzymatic activity, and is, therefore, not necessarily metabolic.<ref name=ref1>PMID:Grassi , F. J., Moretto, N. J., Rivetti, C. J., Cellai, S. J., Betti, M. J., Márquez , A. Ontonello, S. J. (2006). Structural and Functional Properties of Lengsin, a Pseduo-Glutamine Synthetase in the Transparent Human Lens . Retrieved from https://maryville.illiad.oclc.org/illiad/pdf/173917.pdf</ref>
+<scene name='83/837873/Lengsin/4'>Lengsin</scene> (2J9I), is a protein associated with structural formation of the eye. Lengsin has evolutionary relation to <scene name='83/837873/Human_glutamine_synthetase/1'>Glutamine synthetases</scene>, which gives rise to the term lengsin (LENs Glutamine SYNthetase). This protein is specifically classified as a Glutamine Synthetase I, a part of the Glutamine synthetase superfamily. Glutamine synthetases are most well known for their presence in the urea cycle, where they detoxify nitrogen in the body. In other words, Glutamine Synthetases fixate ammonium and create glutamate mechanistically through the utilization of adenosine triphosphate (ATP) and help make the metabolic processes happen. Despite its close relation to this class of enzymes, lengsin, however, does not have any enzymatic activity, and is, therefore, not necessarily metabolic.<ref name=ref1>PMID:Grassi , F. J., Moretto, N. J., Rivetti, C. J., Cellai, S. J., Betti, M. J., Márquez , A. Ontonello, S. J. (2006). Structural and Functional Properties of Lengsin, a Pseduo-Glutamine Synthetase in the Transparent Human Lens . Retrieved from https://maryville.illiad.oclc.org/illiad/pdf/173917.pdf</ref>
 In fact, no catalytic function was present in multiple assays. lengsin was, therefore, declared a noncatalytic dodecamer. Possible reasons for the lack of activity in lengsin could relate to the binding of NH4+ and ATP to the protein, or its inflexibility when transforming to an oligomeric form. Moreover, this protein was first found in a house mouse (mus muluscus) via electron microscopy, and it has been found to have been an important <scene name='83/837873/Evoluntionary_conservation/1'>evolutionary stepping stone</scene> in the formation of the eye lens in several vertebrate species.<ref name=ref1>PMID:Wyatt, K., White, H. E., Wang, L., Bateman, O. A., Slingsby, C., Orlova, E. V., & Wistow, G. (2006). Lengsin is a survivor of an ancient family of class I glutamine synthetases re-engineered by evolution for a role in the vertebrate lens. Structure (London, England : 1993), 14(12), 1823–1834. https://doi.org/10.1016/j.str.2006.10.008</ref>
 Studies have revealed that the evidence for Lengsin’s evolutionary significance lies within the genes which code for this protein. In the N-terminal domain, lies specific exons <ref name=ref2>PMID:Wyatt, K., White, H. E., Wang, L., Bateman, O. A., Slingsby, C., Orlova, E. V., & Wistow, G. (2006). Lengsin is a survivor of an ancient family of class I glutamine synthetases re-engineered by evolution for a role in the vertebrate lens. Structure (London, England : 1993), 14(12), 1823–1834. https://doi.org/10.1016/j.str.2006.10.008</ref>. Through studying the removal and addition of these exons in multiple species, scientists discovered an inactive exon (pseudoexon) in humans which points to clear evolutionary evidence. In many other non-mammalian species, this exon still provides relevance to their overall genome. However, in humans, the pseudoexon is nothing but an extra bit of genetic coding with no known genetic value. For example, comparisons done in fish and birds revealed the activity of multiple exons, including the exon in the n-terminal domain. However, the comparative lengths and numbers  of the exons did change within species. <ref name=ref2>PMID:Wyatt, K., White, H. E., Wang, L., Bateman, O. A., Slingsby, C., Orlova, E. V., & Wistow, G. (2006). Lengsin is a survivor of an ancient family of class I glutamine synthetases re-engineered by evolution for a role in the vertebrate lens. Structure (London, England : 1993), 14(12), 1823–1834. https://doi.org/10.1016/j.str.2006.10.008</ref> The most commonly researched Lengsin dependent species are birds, mice, and fish. Research found that lengsin in zebrafish was about 3,000 base pairs, composed of 4 exons, located on chromosome 11 in the zebrafish embryos. In contrast, mammalian lengsin is approximately 5 exons, located on chromosome 6, so it only shares about 40% genetic similarity to mice and human versions of the protein. <ref name=ref1>PMID:Grassi , F. J., Moretto, N. J., Rivetti, C. J., Cellai, S. J., Betti, M. J., Márquez , A. Ontonello, S. J. (2006). Structural and Functional Properties of Lengsin, a Pseduo-Glutamine Synthetase in the Transparent Human Lens . Retrieved from https://maryville.illiad.oclc.org/illiad/pdf/173917.pdf</ref>  Nonetheless, this protein performs significant tasks in vertebral species by modifying and creating the structure of the lens as well as executing some other specific functions.