Sandbox Reserved 1549
From Proteopedia
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VLCDA clinical mutation can lead to disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue [[1]]. Fatty acids play a crucial role which provides energy for heart and muscle [[2]]. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood [[2]]. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body [[1]]. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype [[2]]. Arg-429 on the helix K makes salt-bridge with Glu-384 on helix I [[2]]. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue [[2]]. Another mutation site is R416H which is found on the helix J [[2]]. Both sites, R429 and R416H, are located close the catalytic glutamate [[2]]. Site R416H has Arg-416 interacts with Asp 391 by making salt bridge and interacts with Gln-395 though hydrogen bond [[2]]. Mutation in R416H causes problem to the position of helix J [[2]]. Furthermore, forming salt bridge with the opposing monomer can affect the dimer interaction [[2]]. | VLCDA clinical mutation can lead to disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue [[1]]. Fatty acids play a crucial role which provides energy for heart and muscle [[2]]. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood [[2]]. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body [[1]]. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype [[2]]. Arg-429 on the helix K makes salt-bridge with Glu-384 on helix I [[2]]. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue [[2]]. Another mutation site is R416H which is found on the helix J [[2]]. Both sites, R429 and R416H, are located close the catalytic glutamate [[2]]. Site R416H has Arg-416 interacts with Asp 391 by making salt bridge and interacts with Gln-395 though hydrogen bond [[2]]. Mutation in R416H causes problem to the position of helix J [[2]]. Furthermore, forming salt bridge with the opposing monomer can affect the dimer interaction [[2]]. | ||
| - | Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases | + | Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases. |
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</StructureSection> | </StructureSection> | ||
| - | == | + | == Notes == |
<references/> | <references/> | ||
| - | 1. VLCAD deficiency - Genetics Home Reference - NIH. (2019, April 02). Retrieved April 30, 2019, from https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency | ||
| - | 2. McAndrew, R. P., Wang, Y., Mohsen, A. W., He, M., Vockley, J., & Kim, J. J. (2008). Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/ | + | == Reference == |
| + | |||
| + | 1. VLCAD deficiency - Genetics Home Reference - NIH. (2019, April 02). Retrieved April 30, 2019, from [https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency] | ||
| + | |||
| + | 2. McAndrew, R. P., Wang, Y., Mohsen, A. W., He, M., Vockley, J., & Kim, J. J. (2008). Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/] | ||
Revision as of 22:47, 30 April 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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Contents |
A Very Long Chain Acyl-CoA Dehydrogenase
|
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.
Function
Disease
VLCDA clinical mutation can lead to disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue 1. Fatty acids play a crucial role which provides energy for heart and muscle 2. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood 2. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body 1. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype 2. Arg-429 on the helix K makes salt-bridge with Glu-384 on helix I 2. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue 2. Another mutation site is R416H which is found on the helix J 2. Both sites, R429 and R416H, are located close the catalytic glutamate 2. Site R416H has Arg-416 interacts with Asp 391 by making salt bridge and interacts with Gln-395 though hydrogen bond 2. Mutation in R416H causes problem to the position of helix J 2. Furthermore, forming salt bridge with the opposing monomer can affect the dimer interaction 2.
Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases.
Structural highlights
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</StructureSection>
Notes
- ↑ 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
- ↑ 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
Reference
1. VLCAD deficiency - Genetics Home Reference - NIH. (2019, April 02). Retrieved April 30, 2019, from [1]
2. McAndrew, R. P., Wang, Y., Mohsen, A. W., He, M., Vockley, J., & Kim, J. J. (2008). Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from [2]
