Sandbox Reserved 1805

From Proteopedia

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== Function of your protein ==
== Function of your protein ==
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MqnA is a chorismate dehydratase that has been studied in Streptomyces coelicolor. MqnA is important because it catalyzes the initial step in the biosynthesis of menaquinone via the futalosine pathway. MqnA folds like a venus flytrap and binds to <scene name='95/954102/Protein_view_2/1'>its substrate.</scene> called chorismate. Without the venus flytrap folding, the protein would be unable to access the binding site. Products of ScMqnA include 3-EPB and the presumed hydrolysis product, 3,4-dihydroxycyclohexa-1,5-dienoate (3,4-CHD).
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MqnA is a chorismate dehydratase that has been studied in Streptomyces coelicolor. MqnA is important because it catalyzes the initial step in the biosynthesis of menaquinone via the futalosine pathway. MqnA folds like a venus flytrap and binds to <scene name='95/954102/Protein_view_2/1'>its substrate</scene> called chorismate. Without the venus flytrap folding, the protein would be unable to access the binding site. Products of ScMqnA include 3-EPB and the presumed hydrolysis product, 3,4-dihydroxycyclohexa-1,5-dienoate (3,4-CHD).
dienoate (3,4-CHD),
dienoate (3,4-CHD),
== Biological relevance and broader implications ==
== Biological relevance and broader implications ==

Revision as of 00:53, 27 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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MqnA Structure

Caption for this structure

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References

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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