Sandbox Reserved 1549: Difference between revisions

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== 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 446-478 are the residue that disordered the VLCAD structure<ref name="Crystal Structure of human very long-chain VLCAD"/>. Due to the proximity of residues both 445 and 479 to the surface, 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"/>.

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 residues both 445 and 479 to the surface, 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 ==

Sandbox Reserved 1549: Difference between revisions

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 == 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 446-478 are the residue that disordered the VLCAD structure<ref name="Crystal Structure of human very long-chain VLCAD"/>. Due to the proximity of residues both 445 and 479 to the surface, 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"/>.
+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 residues both 445 and 479 to the surface, 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 ==