Sandbox Reserved 1544

From Proteopedia

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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.
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.
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Each subunit of a medium-chain acyl-CoA dehydrogenase enzyme is composed of three structural domains. The N-terminal 𝛼-helix domain, the 𝛽-sheet domain, and the C-terminal 𝛼-helix domain.
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== Disease ==
== Disease ==
Medium-chain acyl-CoA dehydrogenase deficiency (MCADD) is a disorder dealing with fatty acid oxidation and can be characterized by hypoglycemic crisis during stressful conditions. MCADD is the most common metabolic defect of fatty acid oxidation. Medium-chain acyl-CoA dehydrogenase is a flavoprotein that catalyzes the first reaction in 𝛽-oxidation of fatty acids. The resulting effects include a decrease of ketone production and an increase in medium-chain fatty acid concentration.
Medium-chain acyl-CoA dehydrogenase deficiency (MCADD) is a disorder dealing with fatty acid oxidation and can be characterized by hypoglycemic crisis during stressful conditions. MCADD is the most common metabolic defect of fatty acid oxidation. Medium-chain acyl-CoA dehydrogenase is a flavoprotein that catalyzes the first reaction in 𝛽-oxidation of fatty acids. The resulting effects include a decrease of ketone production and an increase in medium-chain fatty acid concentration.
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MCADD is passed genetically through an autosomal recessive trait and it is caused by mutations in the medium-chain acyl- CoA dehydrogenase (ACADM) gene. The ACADM gene is located on chromosome 1p31.
== Relevance ==
== Relevance ==

Revision as of 06:01, 12 February 2019

This Sandbox is Reserved from May 28 through July 01, 2019 for use in the course Advanced Biochemistry BCHM 4100 taught by Tom Gluick at the Georgia Gwinnett College. This reservation includes Sandbox Reserved 1544 through Sandbox Reserved 1555.
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Structure

Acyl CoA Dehydrogenase

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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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