Sandbox Reserved 1798: Difference between revisions

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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function of your protein ==

MqnA is found in prokaryotes and eukaryotes: some bacteria, fungi and plants that utilize the futalosine pathway or the shikimate pathway. The Chorismate Dehydratatase MqnA is an enzyme that acts upon chorismate, a biochemical intermediate in plants and microorganisms. On the futalosine pathway, it converts chorismate to EPB by removing water. MqnA is the only known chorismate dehydratase.

You can see the two-part portion of the protein. The protein has been made somewhat<scene name='95/954095/Color_change/5'> transparent</scene> so you can see the substrate within the ligand.

The Chorismate Dehydratatase MqnA is an enzyme that acts upon chorismate, a biochemical intermediate in plants and microorganisms. On the futalosine pathway, it converts chorismate to EPB by removing water. MqnA is the only known chorismate dehydratase.

The futalosine pathway biosynthesizes menaquinone, a carrier of electrons in electron transport chain in prokaryotes. Menaquinone is important for a number of functions in the human body, including cell growth control, apoptosis, and the metabolism of calcium, to name a few. As the human body cannot create menaquinone, it derives it from intestinal bacteria, diet, or by converting plant vitamin K1 (phylloquinone).

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MqnA is relevant to science in that the unique attributes of the protein, such as it’s unique placement in metabolic pathways and Venus fly-trap (VFT) unique structure give much for scientists to digest and theorize about. If the protein is a key piece of a metabolic structure, for example, destruction or inhibition of it can regulate growth of the entire organism.

The mechanics of the protein is studied and compared to similar structures with the VFT in other enzymes like desulfinase DszB, thiamin pyramidine synthase ~~Thi5~~, and thiaminase I. Ordinarily, a rigid portion of the enzyme lobe hinged with another rigid body lobe. The angle of one to the other changes as the ligand is bound and closed or unbound and open. The angle of the hinged motion is from 52 to 37 degrees. Though in other species it can be 7 degrees of motion.

The mechanics of the protein is studied and compared to similar structures with the VFT in other enzymes like desulfinase DszB, thiamin pyramidine synthase The5, and thiaminase I. Ordinarily, a rigid portion of the enzyme lobe hinged with another rigid body lobe. The angle of one to the other changes as the ligand is bound and closed or unbound and open. The angle of the hinged motion is from 52 to 37 degrees. Though in other species it can be 7 degrees of motion.

Different regional amino acids can make the difference in how the mechanism works. The active site of region 109 to 112 can account for the area that will make the most changes in binding if the amino acids are changed. When closed upon each other, the enzymatic mechanism is bound, conversely, when open, unbound.

Sandbox Reserved 1798: Difference between revisions

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@@ Line 5: / Line 5: @@
 You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
 == Function of your protein ==
+MqnA is found in prokaryotes and eukaryotes: some bacteria, fungi and plants that utilize the futalosine pathway or the shikimate pathway. The Chorismate Dehydratatase MqnA is an enzyme that acts upon chorismate, a biochemical intermediate in plants and microorganisms. On the futalosine pathway, it converts chorismate to EPB by removing water.  MqnA is the only known chorismate dehydratase.
 You can see the two-part portion of the protein. The protein has been made somewhat<scene name='95/954095/Color_change/5'> transparent</scene> so you can see the substrate within the ligand.
-The Chorismate Dehydratatase MqnA is an enzyme that acts upon chorismate, a biochemical intermediate in plants and microorganisms. On the futalosine pathway, it converts chorismate to EPB by removing water.  MqnA is the only known chorismate dehydratase.
 The futalosine pathway biosynthesizes menaquinone, a carrier of electrons in electron transport chain in prokaryotes. Menaquinone is important for a number of functions in the human body, including cell growth control, apoptosis, and the metabolism of calcium, to name a few. As the human body cannot create menaquinone, it derives it from intestinal bacteria, diet, or by converting plant vitamin K1 (phylloquinone).
@@ Line 23: / Line 24: @@
 MqnA is relevant to science in that the unique attributes of the protein, such as it’s unique placement in metabolic pathways and Venus fly-trap (VFT) unique structure give much for scientists to digest and theorize about. If the protein is a key piece of a metabolic structure, for example, destruction or inhibition of it can regulate growth of the entire organism.
-The mechanics of the protein is studied and compared to similar structures with the VFT in other enzymes like desulfinase DszB, thiamin pyramidine synthase Thi5, and thiaminase I. Ordinarily, a rigid portion of the enzyme lobe hinged with another rigid body lobe. The angle of one to the other changes as the ligand is bound and closed or unbound and open. The angle of the hinged motion is from 52 to 37 degrees. Though in other species it can be 7 degrees of motion.
+The mechanics of the protein is studied and compared to similar structures with the VFT in other enzymes like desulfinase DszB, thiamin pyramidine synthase The5, and thiaminase I. Ordinarily, a rigid portion of the enzyme lobe hinged with another rigid body lobe. The angle of one to the other changes as the ligand is bound and closed or unbound and open. The angle of the hinged motion is from 52 to 37 degrees. Though in other species it can be 7 degrees of motion.
 Different regional amino acids can make the difference in how the mechanism works. The active site of region 109 to 112 can account for the area that will make the most changes in binding if the amino acids are changed. When closed upon each other, the enzymatic mechanism is bound, conversely, when open, unbound.