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You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
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.
Function
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.
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
Structural highlights
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- ↑ 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:https://dx.doi.org/10.1002/ijch.201300024
- ↑ 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