Sandbox Reserved 1549: Difference between revisions

Line 14:

== Structural highlights ==

VLCAD is a mitochondrial inner-membrane-associated protein and is a homodimer of a 71-kDa polypeptide containing <scene name='80/806435/My_new_scene/1'>2 mol FAD/mol enzyme</scene> <ref name="Souri, M., et al."/>. Both rat and human VLCAD cDNAs encode the entire protein of 655 amino acids, including a 40-amino-acid leader peptide and a 615-amino-acid mature protein <ref name="Souri, M., et al."/>. Three other acyl-CoA dehydrogenases share a high degree of sequence similarity throughout the entire sequences <ref name="Souri, M., et al."/>. VLCAD has a region with a significantly high similarity to other acyl-CoA dehydrogenases at the amino-terminal side, but it has a long tail of approximately 180 amino acid residues at the carboxyl-terminal side, which is not shared with other acyl-CoA dehydrogenases <ref name="Souri, M., et al."/>. Substrate-chain-length specificities of the four acyl-CoA dehydrogenases are different but overlapping <ref name="Souri, M., et al."/>. VLCAD is active toward CoA esters of long-chain and very-long-chain fatty acid <ref name="Souri, M., et al."/>.The overall fold of the N-terminal is about 400 residues of VLCAD is similar to that of the soluble ACADs including medium-chain acyl-CoA dehydrogenase (MCAD) <ref name="Crystal Structure of human very long-chain VLCAD"/>. The novelC-terminal domain forms an -helical bundle that is positioned perpendicular to the two N-terminal helical domains <ref name="Crystal Structure of human very long-chain VLCAD"/>. The fatty acyl moiety of the bound substrate/product is deeply imbedded inside the protein; however, the adenosine pyrophosphate portion of the C14-CoA ligand is disordered because of partial hydrolysis of the thioester bond and high mobility of the CoA moiety <ref name="Crystal Structure of human very long-chain VLCAD"/>.The location of Glu-422with respect to the C2–C3 of the bound ligand and FAD confirms Glu-422 to be the catalytic base <ref name="Crystal Structure of human very long-chain VLCAD"/>. In MCAD, Gln-95 and Glu-99 form the base of the substrate binding cavity <ref name="Crystal Structure of human very long-chain VLCAD"/>. In VLCAD, these residues are glycines (Gly-175 andGly-178), allowing the binding channel to extend for an additional 12 A ˚ and permitting substrate acyl chain lengths as long as 24 carbons <ref name="Crystal Structure of human very long-chain VLCAD"/>.

VLCAD is a mitochondrial inner-membrane-associated protein and is a homodimer of a 71-kDa polypeptide containing <scene name='80/806435/My_new_scene/1'>2 mol FAD/mol enzyme</scene> <ref name="Souri, M., et al."/>. Both rat and human VLCAD cDNAs encode the entire protein of 655 amino acids, including a 40-amino-acid leader peptide and a 615-amino-acid mature protein <ref name="Souri, M., et al."/>. Three other acyl-CoA dehydrogenases share a high degree of sequence similarity throughout the entire sequences <ref name="Souri, M., et al."/>. VLCAD has a region with a significantly high similarity to other acyl-CoA dehydrogenases at the amino-terminal side, but it has a long tail of approximately 180 amino acid residues at the carboxyl-terminal side, which is not shared with other acyl-CoA dehydrogenases <ref name="Souri, M., et al."/>. Substrate-chain-length specificities of the four acyl-CoA dehydrogenases are different but overlapping <ref name="Souri, M., et al."/>. VLCAD is active toward CoA esters of long-chain and very-long-chain fatty acid <ref name="Souri, M., et al."/>.The overall fold of the N-terminal is about 400 residues of VLCAD is similar to that of the soluble ACADs including medium-chain acyl-CoA dehydrogenase (MCAD) <ref name="Crystal Structure of human very long-chain VLCAD"/>. The novelC-terminal domain forms an -helical bundle that is positioned perpendicular to the two N-terminal helical domains <ref name="Crystal Structure of human very long-chain VLCAD"/>. The fatty acyl moiety of the bound substrate/product is deeply imbedded inside the protein; however, the adenosine pyrophosphate portion of the C14-CoA ligand is disordered because of partial hydrolysis of the thioester bond and high mobility of the CoA moiety <ref name="Crystal Structure of human very long-chain VLCAD"/>.The location of Glu-422with respect to the C2–C3 of the bound ligand and<scene name='80/806435/Fad/1'> FAD confirms Glu-422 to be the catalytic base</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. In MCAD, Gln-95 and Glu-99 form the base of the substrate binding cavity <ref name="Crystal Structure of human very long-chain VLCAD"/>. In VLCAD, these residues are glycines (Gly-175 andGly-178), allowing the binding channel to extend for an additional 12 A ˚ and permitting substrate acyl chain lengths as long as 24 carbons <ref name="Crystal Structure of human very long-chain VLCAD"/>.

== Reference ==

Sandbox Reserved 1549: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 14: / Line 14: @@
 == Structural highlights ==
-VLCAD is a mitochondrial inner-membrane-associated protein and is a homodimer of a 71-kDa polypeptide containing <scene name='80/806435/My_new_scene/1'>2 mol FAD/mol enzyme</scene> <ref name="Souri, M., et al."/>. Both rat and human VLCAD cDNAs encode the entire protein of 655 amino acids, including a 40-amino-acid leader peptide and a 615-amino-acid mature protein <ref name="Souri, M., et al."/>. Three other acyl-CoA dehydrogenases share a high degree of sequence similarity throughout the entire sequences <ref name="Souri, M., et al."/>. VLCAD has a region with a significantly high similarity to other acyl-CoA dehydrogenases at the amino-terminal side, but it has a long tail of approximately 180 amino acid residues at the carboxyl-terminal side, which is not shared with other acyl-CoA dehydrogenases <ref name="Souri, M., et al."/>. Substrate-chain-length specificities of the four acyl-CoA dehydrogenases are different but overlapping <ref name="Souri, M., et al."/>. VLCAD is active toward CoA esters of long-chain and very-long-chain fatty acid <ref name="Souri, M., et al."/>.The overall fold of the N-terminal is about 400 residues of VLCAD is similar to that of the soluble ACADs including medium-chain acyl-CoA dehydrogenase (MCAD) <ref name="Crystal Structure of human very long-chain VLCAD"/>. The novelC-terminal domain forms an   -helical bundle that is positioned perpendicular to the two N-terminal helical domains <ref name="Crystal Structure of human very long-chain VLCAD"/>. The fatty acyl moiety of the bound substrate/product is deeply imbedded inside the protein; however, the adenosine pyrophosphate portion of the C14-CoA ligand is disordered because of partial hydrolysis of the thioester bond and high mobility of the CoA moiety <ref name="Crystal Structure of human very long-chain VLCAD"/>.The location of Glu-422with respect to the C2–C3 of the bound ligand and FAD confirms Glu-422 to be the catalytic base <ref name="Crystal Structure of human very long-chain VLCAD"/>. In MCAD, Gln-95 and Glu-99 form the base of the substrate binding cavity <ref name="Crystal Structure of human very long-chain VLCAD"/>. In VLCAD, these residues are glycines (Gly-175 andGly-178), allowing the binding channel to extend for an additional 12 A ˚ and permitting substrate acyl chain lengths as long as 24 carbons <ref name="Crystal Structure of human very long-chain VLCAD"/>.
+VLCAD is a mitochondrial inner-membrane-associated protein and is a homodimer of a 71-kDa polypeptide containing <scene name='80/806435/My_new_scene/1'>2 mol FAD/mol enzyme</scene> <ref name="Souri, M., et al."/>. Both rat and human VLCAD cDNAs encode the entire protein of 655 amino acids, including a 40-amino-acid leader peptide and a 615-amino-acid mature protein <ref name="Souri, M., et al."/>. Three other acyl-CoA dehydrogenases share a high degree of sequence similarity throughout the entire sequences <ref name="Souri, M., et al."/>. VLCAD has a region with a significantly high similarity to other acyl-CoA dehydrogenases at the amino-terminal side, but it has a long tail of approximately 180 amino acid residues at the carboxyl-terminal side, which is not shared with other acyl-CoA dehydrogenases <ref name="Souri, M., et al."/>. Substrate-chain-length specificities of the four acyl-CoA dehydrogenases are different but overlapping <ref name="Souri, M., et al."/>. VLCAD is active toward CoA esters of long-chain and very-long-chain fatty acid <ref name="Souri, M., et al."/>.The overall fold of the N-terminal is about 400 residues of VLCAD is similar to that of the soluble ACADs including medium-chain acyl-CoA dehydrogenase (MCAD) <ref name="Crystal Structure of human very long-chain VLCAD"/>. The novelC-terminal domain forms an   -helical bundle that is positioned perpendicular to the two N-terminal helical domains <ref name="Crystal Structure of human very long-chain VLCAD"/>. The fatty acyl moiety of the bound substrate/product is deeply imbedded inside the protein; however, the adenosine pyrophosphate portion of the C14-CoA ligand is disordered because of partial hydrolysis of the thioester bond and high mobility of the CoA moiety <ref name="Crystal Structure of human very long-chain VLCAD"/>.The location of Glu-422with respect to the C2–C3 of the bound ligand and<scene name='80/806435/Fad/1'> FAD confirms Glu-422 to be the catalytic base</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. In MCAD, Gln-95 and Glu-99 form the base of the substrate binding cavity <ref name="Crystal Structure of human very long-chain VLCAD"/>. In VLCAD, these residues are glycines (Gly-175 andGly-178), allowing the binding channel to extend for an additional 12 A ˚ and permitting substrate acyl chain lengths as long as 24 carbons <ref name="Crystal Structure of human very long-chain VLCAD"/>.
 == Reference ==