Sandbox Reserved 1549: Difference between revisions

Line 5:

== 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"/>.

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 (Gly-135 and Gly—139), 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

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 5: / Line 5: @@
 == 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"/>.
+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 (Gly-135 and Gly—139), in which efficiently open up and deepen the binding pocket<ref name="Crystal Structure of human very long-chain VLCAD"/>.
 == Disease ==