Proteopedia - User contributions [en]

Sandbox Reserved 1549

2019-05-01T19:42:29Z

Uyen Chu:

{{ Sandbox_Reserved_GGC_BHCM4100_1}}
==A Very Long Chain Acyl-CoA Dehydrogenase==
<Structure load='3B96' size='300' frame='true' align='right' caption='' scene='Very Long Chain Acyl-CoA Dehydrogenase'/>
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 ==
Very long-chain acyl-CoA dehydrogenase (VLCAD) is one of the five members of acyl-CoA dehydrogenases (ACADs). VLCADs assembles the initial, rate limiting step of mitochondrial fatty acid β-oxidation<ref name="Crystal Structure of human very long-chain VLCAD"/>. The VLCAD has ideal chain length specificity in which fatty acyl-CoA has 16 carbons in length<ref name="Crystal Structure of human very long-chain VLCAD"/>. They are long-, medium-, and short-chain acyl CoA dehydrogenase<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, the activation of acyl CoA dehydrogenase 9 (ACAD-9) is mostly with unsaturated long-chain acyl-CoAs<ref name="Crystal Structure of human very long-chain VLCAD"/>. Unlike other ACADs, mature VLCAD and ACAD-9 are homodimers of 67-kDa subunit which binds to the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. VLCAD and ACAD- 9 possess an additional 180 residues on the C-terminal end, and also with other AVCADs, they possess MCAD-like catalytic glutamate<ref name="Crystal Structure of human very long-chain VLCAD"/>. In fact, not only allows longer chain-length substrates to bind, VLCAD prefers them to bind<ref name="Crystal Structure of human very long-chain VLCAD"/>. C-terminal domain of VLCAD has shown to be subjected for binding to the matrix side of the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. A450P and L462P are human clinical mutants in which located in the C-terminal domain. When these mutants are active and stable, it is reducing the capability to bind the membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. However, there is no clear hydrophobic patch visible that can interact with the membrane, and <scene name='80/806435/Res446/1'>residues 446-478</scene> are the residue that disordered the VLCAD structure<ref name="Crystal Structure of human very long-chain VLCAD"/>. Due to the proximity of <scene name='80/806435/445/1'>residues both 445 and 479 to the surface</scene>, and it expects that the disordered residues occur at the surface of the molecule<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, there are Gln-95 and Glu-99, in which located in MCAD, they help to form the base of the building cavity<ref name="Crystal Structure of human very long-chain VLCAD"/>. In VLCAD, these residues are called glycine (<scene name='80/806435/Gly/1'>Gly-135 and Gly—139</scene>), in which efficiently open up and deepen the binding pocket<ref name="Crystal Structure of human very long-chain VLCAD"/>.

== Disease ==
VLCDA clinical mutation can lead to a disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue <ref name="VLCAD deficiency">VLCAD deficiency - Genetics Home Reference https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency</ref>. Fatty acids play a crucial role which provides energy for heart and muscle <ref name="Crystal Structure of human very long-chain VLCAD"/>. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood <ref name="Crystal Structure of human very long-chain VLCAD">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/</ref>. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body <ref name="VLCAD deficiency"/>. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype <ref name="Crystal Structure of human very long-chain VLCAD"/>. <scene name='80/806435/Helixk/1'>Arg-429</scene> on the helix K makes salt-bridge with <scene name='80/806435/Helixk/1'>Glu-384</scene> on helix I <ref name="Crystal Structure of human very long-chain VLCAD"/>. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue <ref name="Crystal Structure of human very long-chain VLCAD"/>. Another mutation site is R416H which is found on the helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Both sites,<scene name='80/806435/Gln422/1'> R429W and R416H</scene>, are located close to the <scene name='80/806435/Gln422/1'> catalytic glutamate</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Site R416H has <scene name='80/806435/Helixj/1'>Arg-416 interacts with Asp-391</scene> by making salt bridge and interacts <scene name='80/806435/Helixj/1'>Gln-395 </scene> through hydrogen bond <ref name="Crystal Structure of human very long-chain VLCAD"/>. Mutation in R416H causes the problem to the position of helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Furthermore, forming a salt bridge with the opposing monomer can affect the dimer interaction <ref name="Crystal Structure of human very long-chain VLCAD"/>.

Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases <ref name="VLCAD deficiency"/>.

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== Notes ==
<references/>

== 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/

Sandbox Reserved 1549

2019-05-01T15:17:00Z

Uyen Chu:

{{ Sandbox_Reserved_GGC_BHCM4100_1}}
==A Very Long Chain Acyl-CoA Dehydrogenase==
<Structure load='3B96' size='300' frame='true' align='right' caption='' scene='Very Long Chain Acyl-CoA Dehydrogenase'/>
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 ==
Very long-chain acyl-CoA dehydrogenase (VLCAD) is one of the five members of acyl-CoA dehydrogenases (ACADs). VLCADs assembles the initial, rate limiting step of mitochondrial fatty acid β-oxidation<ref name="Crystal Structure of human very long-chain VLCAD"/>. The VLCAD has ideal chain length specificity in which fatty acyl-CoA has 16 carbons in length. They are long-, medium-, and short-chain acyl CoA dehydrogenase<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, the activation of acyl CoA dehydrogenase 9 (ACAD-9) is mostly with unsaturated long-chain acyl-CoAs. Unlike other ACADs, mature VLCAD and ACAD-9 are homodimers of 67-kDa subunit which binds to the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. VLCAD and ACAD- 9 possess an additional 180 residues on the C-terminal end, and also with other AVCADs, they possess MCAD-like catalytic glutamate<ref name="Crystal Structure of human very long-chain VLCAD"/>. In fact, not only allows longer chain-length substrates to bind, VLCAD prefers them to bind<ref name="Crystal Structure of human very long-chain VLCAD"/>. C-terminal domain of VLCAD has shown to be subjected for binding to the matrix side of the inner mitochondrial membrane. A450P and L462P are human clinical mutants in which located in the C-terminal domain. When these mutants are active and stable, it is reducing the capability to bind the membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>.

== Disease ==
VLCDA clinical mutation can lead to a disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue <ref name="VLCAD deficiency">VLCAD deficiency - Genetics Home Reference https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency</ref>. Fatty acids play a crucial role which provides energy for heart and muscle <ref name="Crystal Structure of human very long-chain VLCAD"/>. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood <ref name="Crystal Structure of human very long-chain VLCAD">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/</ref>. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body <ref name="VLCAD deficiency"/>. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype <ref name="Crystal Structure of human very long-chain VLCAD"/>. <scene name='80/806435/Helixk/1'>Arg-429</scene> on the helix K makes salt-bridge with <scene name='80/806435/Helixk/1'>Glu-384</scene> on helix I <ref name="Crystal Structure of human very long-chain VLCAD"/>. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue <ref name="Crystal Structure of human very long-chain VLCAD"/>. Another mutation site is R416H which is found on the helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Both sites,<scene name='80/806435/Gln422/1'> R429W and R416H</scene>, are located close to the <scene name='80/806435/Gln422/1'> catalytic glutamate</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Site R416H has <scene name='80/806435/Helixj/1'>Arg-416 interacts with Asp-391 by making salt bridge</scene> and interacts <scene name='80/806435/Helixj/1'>Gln-395 through hydrogen bond</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Mutation in R416H causes the problem to the position of helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Furthermore, forming a salt bridge with the opposing monomer can affect the dimer interaction <ref name="Crystal Structure of human very long-chain VLCAD"/>.

Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases <ref name="VLCAD deficiency"/>.

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== Notes ==
<references/>

== 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/

Sandbox Reserved 1549

2019-05-01T04:03:01Z

Uyen Chu:

{{ Sandbox_Reserved_GGC_BHCM4100_1}}
==A Very Long Chain Acyl-CoA Dehydrogenase==
<Structure load='3B96' size='300' frame='true' align='right' caption='' scene='Very Long Chain Acyl-CoA Dehydrogenase' />
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 ==
Very long-chain acyl-CoA dehydrogenase (VLCAD) is one of the five members of acyl-CoA dehydrogenases (ACADs). VLCADs assembles the initial, rate limiting step of mitochondrial fatty acid β-oxidation<ref name="Crystal Structure of human very long-chain VLCAD"/>. The VLCAD has ideal chain length specificity in which fatty acyl-CoA has 16 carbons in length. They are long-, medium-, and short-chain acyl CoA dehydrogenase<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, the activation of acyl CoA dehydrogenase 9 (ACAD-9) is mostly with unsaturated long-chain acyl-CoAs. Unlike other ACADs, mature VLCAD and ACAD-9 are homodimers of 67-kDa subunit which binds to the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. VLCAD and ACAD- 9 possess an additional 180 residues on the C-terminal end, and also with other AVCADs, they possess MCAD-like catalytic glutamate<ref name="Crystal Structure of human very long-chain VLCAD"/>. In fact, not only allows longer chain-length substrates to bind, VLCAD prefers them to bind<ref name="Crystal Structure of human very long-chain VLCAD"/>. C-terminal domain of VLCAD has shown to be subjected for binding to the matrix side of the inner mitochondrial membrane. A450P and L4462P are human clinical mutants in which located in the C-terminal domain. When these mutants are active and stable, it is reducing the capability to bind the membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>.

== Disease ==
VLCDA clinical mutation can lead to a disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue <ref name="VLCAD deficiency">VLCAD deficiency - Genetics Home Reference https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency</ref>. Fatty acids play a crucial role which provides energy for heart and muscle <ref name="Crystal Structure of human very long-chain VLCAD"/>. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood <ref name="Crystal Structure of human very long-chain VLCAD">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/</ref>. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body <ref name="VLCAD deficiency"/>. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype <ref name="Crystal Structure of human very long-chain VLCAD"/>. <scene name='80/806435/Helixk/1'>Arg-429</scene> on the helix K makes salt-bridge with <scene name='80/806435/Helixk/1'>Glu-384</scene> on helix I <ref name="Crystal Structure of human very long-chain VLCAD"/>. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue <ref name="Crystal Structure of human very long-chain VLCAD"/>. Another mutation site is R416H which is found on the helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Both sites,<scene name='80/806435/Gln422/1'> R429W and R416H</scene>, are located close to the <scene name='80/806435/Gln422/1'> catalytic glutamate</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Site R416H has <scene name='80/806435/Helixj/1'>Arg-416 interacts with Asp-391 by making salt bridge</scene> and interacts <scene name='80/806435/Helixj/1'>Gln-395 through hydrogen bond</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Mutation in R416H causes the problem to the position of helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Furthermore, forming a salt bridge with the opposing monomer can affect the dimer interaction <ref name="Crystal Structure of human very long-chain VLCAD"/>.

Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases <ref name="VLCAD deficiency"/>.

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== Notes ==
<references/>

== 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/

Sandbox Reserved 1549

2019-05-01T04:00:56Z

Uyen Chu:

{{ Sandbox_Reserved_GGC_BHCM4100_1}}
==A Very Long Chain Acyl-CoA Dehydrogenase==
<Structure load='3B96' size='300' frame='true' align='right' caption='' scene='Very Long Chain Acyl-CoA Dehydrogenase' />
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 ==
Very long-chain acyl-CoA dehydrogenase (VLCAD) is one of the five members of acyl-CoA dehydrogenases (ACADs). VLCADs assembles the initial, rate limiting step of mitochondrial fatty acid β-oxidation<ref name="Crystal Structure of human very long-chain VLCAD"/>. The VLCAD has ideal chain length specificity in which fatty acyl-CoA has 16 carbons in length. They are long-, medium-, and short-chain acyl CoA dehydrogenase<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, the activation of acyl CoA dehydrogenase 9 (ACAD-9) is mostly with unsaturated long-chain acyl-CoAs. Unlike other ACADs, mature VLCAD and ACAD-9 are homodimers of 67-kDa subunit which binds to the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. VLCAD and ACAD- 9 possess an additional 180 residues on the C-terminal end, and also with other AVCADs, they possess MCAD-like catalytic glutamate<ref name="Crystal Structure of human very long-chain VLCAD"/>. In fact, not only allows longer chain-length substrates to bind, VLCAD prefers them to bind<ref name="Crystal Structure of human very long-chain VLCAD"/>. C-terminal domain of VLCAD has shown to be subjected for binding to the matrix side of the inner mitochondrial membrane. A450P and L4462P are human clinical mutants in which located in the C-terminal domain. When these mutants are active and stable, it is reducing the capability to bind the membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>.

== Disease ==
VLCDA clinical mutation can lead to a disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue <ref name="VLCAD deficiency">VLCAD deficiency - Genetics Home Reference https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency</ref>. Fatty acids play a crucial role which provides energy for heart and muscle <ref name="Crystal Structure of human very long-chain VLCAD"/>. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood <ref name="Crystal Structure of human very long-chain VLCAD">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/</ref>. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body <ref name="VLCAD deficiency"/>. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype <ref name="Crystal Structure of human very long-chain VLCAD"/>. <scene name='80/806435/Helixk/1'>Arg-429</scene> on the helix K makes salt-bridge with <scene name='80/806435/Helixk/1'>Glu-384</scene> on helix I <ref name="Crystal Structure of human very long-chain VLCAD"/>. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue <ref name="Crystal Structure of human very long-chain VLCAD"/>. Another mutation site is R416H which is found on the helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Both sites,<scene name='80/806435/Gln422/1'> R429 and R416H</scene>, are located close to the <scene name='80/806435/Gln422/1'> catalytic glutamate</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Site R416H has <scene name='80/806435/Helixj/1'>Arg-416 interacts with Asp-391 by making salt bridge</scene> and interacts <scene name='80/806435/Helixj/1'>Gln-395 through hydrogen bond</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Mutation in R416H causes the problem to the position of helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Furthermore, forming a salt bridge with the opposing monomer can affect the dimer interaction <ref name="Crystal Structure of human very long-chain VLCAD"/>.

Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases <ref name="VLCAD deficiency"/>.

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== Notes ==
<references/>

== 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/

Sandbox Reserved 1549

2019-05-01T03:58:32Z

Uyen Chu:

{{ Sandbox_Reserved_GGC_BHCM4100_1}}
==A Very Long Chain Acyl-CoA Dehydrogenase==
<Structure load='3B96' size='300' frame='true' align='right' caption='' scene='Very Long Chain Acyl-CoA Dehydrogenase' />
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 ==
Very long-chain acyl-CoA dehydrogenase (VLCAD) is one of the five members of acyl-CoA dehydrogenases (ACADs). VLCADs assembles the initial, rate limiting step of mitochondrial fatty acid β-oxidation<ref name="Crystal Structure of human very long-chain VLCAD"/>. The VLCAD has ideal chain length specificity in which fatty acyl-CoA has 16 carbons in length. They are long-, medium-, and short-chain acyl CoA dehydrogenase<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, the activation of acyl CoA dehydrogenase 9 (ACAD-9) is mostly with unsaturated long-chain acyl-CoAs. Unlike other ACADs, mature VLCAD and ACAD-9 are homodimers of 67-kDa subunit which binds to the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. VLCAD and ACAD- 9 possess an additional 180 residues on the C-terminal end, and also with other AVCADs, they possess MCAD-like catalytic glutamate<ref name="Crystal Structure of human very long-chain VLCAD"/>. In fact, not only allows longer chain-length substrates to bind, VLCAD prefers them to bind<ref name="Crystal Structure of human very long-chain VLCAD"/>. C-terminal domain of VLCAD has shown to be subjected for binding to the matrix side of the inner mitochondrial membrane. A450P and L4462P are human clinical mutants in which located in the C-terminal domain. When these mutants are active and stable, it is reducing the capability to bind the membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>.

== Disease ==
VLCDA clinical mutation can lead to a disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue <ref name="VLCAD deficiency">VLCAD deficiency - Genetics Home Reference https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency</ref>. Fatty acids play a crucial role which provides energy for heart and muscle <ref name="Crystal Structure of human very long-chain VLCAD"/>. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood <ref name="Crystal Structure of human very long-chain VLCAD">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/</ref>. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body <ref name="VLCAD deficiency"/>. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype <ref name="Crystal Structure of human very long-chain VLCAD"/>. <scene name='80/806435/Helixk/1'>Arg-429</scene> on the helix K makes salt-bridge with <scene name='80/806435/Helixk/1'>Glu-384</scene> on helix I <ref name="Crystal Structure of human very long-chain VLCAD"/>. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue <ref name="Crystal Structure of human very long-chain VLCAD"/>. Another mutation site is R416H which is found on the helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Both sites,<scene name='80/806435/Gln422/1'> R429 and R416H</scene>, are located close to the <scene name='80/806435/Gln422/1'> catalytic glutamate</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Site R416H has <scene name='80/806435/Helixj/1'>Arg-416 interacts with Asp-391 by making salt bridge</scene> and interacts with through hydrogen bond <scene name='80/806435/Helixj/1'>Gln-395 through hydrogen bond</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Mutation in R416H causes the problem to the position of helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Furthermore, forming a salt bridge with the opposing monomer can affect the dimer interaction <ref name="Crystal Structure of human very long-chain VLCAD"/>.

Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases <ref name="VLCAD deficiency"/>.

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== Notes ==
<references/>

== 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/

Sandbox Reserved 1549

2019-05-01T03:38:42Z

Uyen Chu:

{{ Sandbox_Reserved_GGC_BHCM4100_1}}
==A Very Long Chain Acyl-CoA Dehydrogenase==
<Structure load='3B96' size='300' frame='true' align='right' caption='' scene='Very Long Chain Acyl-CoA Dehydrogenase' />
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 ==
Very long-chain acyl-CoA dehydrogenase (VLCAD) is one of the five members of acyl-CoA dehydrogenases (ACADs). VLCADs assembles the initial, rate limiting step of mitochondrial fatty acid β-oxidation<ref name="Crystal Structure of human very long-chain VLCAD"/>. The VLCAD has ideal chain length specificity in which fatty acyl-CoA has 16 carbons in length. They are long-, medium-, and short-chain acyl CoA dehydrogenase<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, the activation of acyl CoA dehydrogenase 9 (ACAD-9) is mostly with unsaturated long-chain acyl-CoAs. Unlike other ACADs, mature VLCAD and ACAD-9 are homodimers of 67-kDa subunit which binds to the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. VLCAD and ACAD- 9 possess an additional 180 residues on the C-terminal end, and also with other AVCADs, they possess MCAD-like catalytic glutamate<ref name="Crystal Structure of human very long-chain VLCAD"/>. In fact, not only allows longer chain-length substrates to bind, VLCAD prefers them to bind<ref name="Crystal Structure of human very long-chain VLCAD"/>. C-terminal domain of VLCAD has shown to be subjected for binding to the matrix side of the inner mitochondrial membrane. A450P and L4462P are human clinical mutants in which located in the C-terminal domain. When these mutants are active and stable, it is reducing the capability to bind the membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>.

== Disease ==
VLCDA clinical mutation can lead to a disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue <ref name="VLCAD deficiency">VLCAD deficiency - Genetics Home Reference https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency</ref>. Fatty acids play a crucial role which provides energy for heart and muscle <ref name="Crystal Structure of human very long-chain VLCAD"/>. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood <ref name="Crystal Structure of human very long-chain VLCAD">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/</ref>. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body <ref name="VLCAD deficiency"/>. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype <ref name="Crystal Structure of human very long-chain VLCAD"/>. <scene name='80/806435/Helixk/1'>Arg-429</scene> on the helix K makes salt-bridge with <scene name='80/806435/Helixk/1'>Glu-384</scene> on helix I <ref name="Crystal Structure of human very long-chain VLCAD"/>. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue <ref name="Crystal Structure of human very long-chain VLCAD"/>. Another mutation site is R416H which is found on the helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Both sites, R429 and R416H, are located close to the catalytic glutamate <ref name="Crystal Structure of human very long-chain VLCAD"/>. Site R416H has <scene name='80/806435/Helixj/1'>Arg-416 interacts with Asp-391 by making salt bridge</scene> and interacts with through hydrogen bond <scene name='80/806435/Helixj/1'>Gln-395 through hydrogen bond</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Mutation in R416H causes the problem to the position of helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Furthermore, forming a salt bridge with the opposing monomer can affect the dimer interaction <ref name="Crystal Structure of human very long-chain VLCAD"/>.

Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases <ref name="VLCAD deficiency"/>.

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== Notes ==
<references/>

== 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/

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Uyen Chu:

{{ Sandbox_Reserved_GGC_BHCM4100_1}}
==A Very Long Chain Acyl-CoA Dehydrogenase==
<Structure load='3B96' size='300' frame='true' align='right' caption='' scene='Very Long Chain Acyl-CoA Dehydrogenase' />
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 ==
Very long-chain acyl-CoA dehydrogenase (VLCAD) is one of the five members of acyl-CoA dehydrogenases (ACADs). VLCADs assembles the initial, rate limiting step of mitochondrial fatty acid β-oxidation<ref name="Crystal Structure of human very long-chain VLCAD"/>. The VLCAD has ideal chain length specificity in which fatty acyl-CoA has 16 carbons in length. They are long-, medium-, and short-chain acyl CoA dehydrogenase<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, the activation of acyl CoA dehydrogenase 9 (ACAD-9) is mostly with unsaturated long-chain acyl-CoAs. Unlike other ACADs, mature VLCAD and ACAD-9 are homodimers of 67-kDa subunit which binds to the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. VLCAD and ACAD- 9 possess an additional 180 residues on the C-terminal end, and also with other AVCADs, they possess MCAD-like catalytic glutamate<ref name="Crystal Structure of human very long-chain VLCAD"/>. In fact, not only allows longer chain-length substrates to bind, VLCAD prefers them to bind<ref name="Crystal Structure of human very long-chain VLCAD"/>. C-terminal domain of VLCAD has shown to be subjected for binding to the matrix side of the inner mitochondrial membrane. A450P and L4462P are human clinical mutants in which located in the C-terminal domain. When these mutants are active and stable, it is reducing the capability to bind the membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>.

== Disease ==
VLCDA clinical mutation can lead to a disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue <ref name="VLCAD deficiency">VLCAD deficiency - Genetics Home Reference https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency</ref>. Fatty acids play a crucial role which provides energy for heart and muscle <ref name="Crystal Structure of human very long-chain VLCAD"/>. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood <ref name="Crystal Structure of human very long-chain VLCAD">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/</ref>. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body <ref name="VLCAD deficiency"/>. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype <ref name="Crystal Structure of human very long-chain VLCAD"/>. <scene name='80/806435/Helixk/1'>Arg-429</scene> on the helix K makes salt-bridge with <scene name='80/806435/Helixk/1'>Glu-384</scene> on helix I <ref name="Crystal Structure of human very long-chain VLCAD"/>. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue <ref name="Crystal Structure of human very long-chain VLCAD"/>. Another mutation site is R416H which is found on the helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Both sites, R429 and R416H, are located close to the catalytic glutamate <ref name="Crystal Structure of human very long-chain VLCAD"/>. Site R416H has Arg-416 interacts with Asp 391 by making salt bridge and interacts with Gln-395 through hydrogen bond <ref name="Crystal Structure of human very long-chain VLCAD"/>. Mutation in R416H causes the problem to the position of helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Furthermore, forming a salt bridge with the opposing monomer can affect the dimer interaction <ref name="Crystal Structure of human very long-chain VLCAD"/>.

Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases <ref name="VLCAD deficiency"/>.

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== Notes ==
<references/>

== 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/

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