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. 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"/>. ~~VLCAD is a monotopic membrane protein, and its~~ 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"/>.

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 ==

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. 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"/>. VLCAD is a monotopic membrane protein, and its 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"/>.
+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 ==