Sandbox Reserved 1797

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== Function of your protein ==
== Function of your protein ==
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<scene name='95/954094/Less_protein/1'>LdmS</scene> is found in Staphylococcus aureus. It exists in an open state but, can also be seen modified to a closed state. It has related mechanisms to different ATP-grasp enzymes just with different active sites. LdmS main function is to aid in the metabolism of Staphylococcal sulfur amino acids by specifically controlling Met and Cys metabolism . It can still function in settings with a lot of nutrients, or hardly any at all. This is very bad for the person infected with Staph. It's known substrates are L-Met and L-Asp. It is a receptor and interacts with ADP and citrate. <ref>DOI:https://doi.org/10.1016/j.jbc.2022.102392</ref>
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<scene name='95/954094/Less_protein/1'>LdmS</scene> is found in Staphylococcus aureus. It exists in an open state but, can also be seen modified to a closed state. It has related mechanisms to different ATP-grasp enzymes just with different active sites. LdmS main function is to aid in the metabolism of Staphylococcal sulfur amino acids by specifically controlling Met and Cys metabolism . It can still function in settings with a lot of nutrients, or hardly any at all. This is very bad for the person infected with Staph. It's known substrates are L-Met and L-Asp. It is a receptor and interacts with ADP and citrate. <ref>PMID:35988643</ref>
== Biological relevance and broader implications ==
== Biological relevance and broader implications ==
LdmS is important to the biology of humans. Staph infection is a serious disease that can become resistant to antibiotics making it difficult to treat (Mayo, n.d.). It is important to study how LdmS can metabolize Staphylococcal so that we can monitor how it is mutating against antibiotics. We can also see how LdmS may help with creating stronger, more resistant antibiotics for future use.
LdmS is important to the biology of humans. Staph infection is a serious disease that can become resistant to antibiotics making it difficult to treat (Mayo, n.d.). It is important to study how LdmS can metabolize Staphylococcal so that we can monitor how it is mutating against antibiotics. We can also see how LdmS may help with creating stronger, more resistant antibiotics for future use.
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LdmS is relevant to any disease that is catalyzed by Met and Cys, which helps host the disease in the body. <ref>DOI:https://doi.org/10.1016/j.jbc.2022.102392</ref>
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LdmS is relevant to any disease that is catalyzed by Met and Cys, which helps host the disease in the body. <ref>PMID:35988643</ref>
== Important amino acids==
== Important amino acids==
<scene name='95/954094/Ligand/1'>The ligands</scene> are there to facilitate binding at the active sites to further catalyze the metabolism. The <scene name='95/954094/Polar_sites/1'>polar</scene> cavity and <scene name='95/954094/Hydrophobic_sites/1'>hydrophobic</scene> cavity are indicated here. These sites help the protein bind to other atoms even in an aqueous solutions. The hydrophobic sites are actually inside of the protein so that they do not interact with the aqueous solution.
<scene name='95/954094/Ligand/1'>The ligands</scene> are there to facilitate binding at the active sites to further catalyze the metabolism. The <scene name='95/954094/Polar_sites/1'>polar</scene> cavity and <scene name='95/954094/Hydrophobic_sites/1'>hydrophobic</scene> cavity are indicated here. These sites help the protein bind to other atoms even in an aqueous solutions. The hydrophobic sites are actually inside of the protein so that they do not interact with the aqueous solution.

Revision as of 00:57, 28 April 2023

This Sandbox is Reserved from Mar 1 through Jun 1, 2023 for use in the course CHEM 351 Biochemistry taught by Bonnie_Hall at the Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1796 through Sandbox Reserved 1811.
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ʟ-aspartate–ʟ-methionine ligase (LdmS)(7r8p)

LdmS

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References

  1. Pederick JL, Horsfall AJ, Jovcevski B, Klose J, Abell AD, Pukala TL, Bruning JB. Discovery of an L-amino acid ligase implicated in Staphylococcal sulfur amino acid metabolism. J Biol Chem. 2022 Aug 18:102392. doi: 10.1016/j.jbc.2022.102392. PMID:35988643 doi:http://dx.doi.org/10.1016/j.jbc.2022.102392
  2. Pederick JL, Horsfall AJ, Jovcevski B, Klose J, Abell AD, Pukala TL, Bruning JB. Discovery of an L-amino acid ligase implicated in Staphylococcal sulfur amino acid metabolism. J Biol Chem. 2022 Aug 18:102392. doi: 10.1016/j.jbc.2022.102392. PMID:35988643 doi:http://dx.doi.org/10.1016/j.jbc.2022.102392
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