Carnitine palmitoyltransferase
From Proteopedia
(Difference between revisions)
| (18 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | + | <StructureSection load='2rcu' size='350' side='right' scene='48/485614/Cv1/1' caption='Rat carnitine palmitoyltransferase II dimer complex with substrate analog and octylglucoside (PDB code [[2rcu]])'> | |
| + | __TOC__ | ||
| + | == Function == | ||
| - | + | '''Carnitine palmitoyltransferase''' (CPT I and CPT II) are involved in the transport of long-chain fatty acids into the mitochondria where they are oxidized. Fatty acids form a conjugate with CoA before being oxidized in the mitochondria. However, the CoA-long-chain fatty acid conjugates can not diffuse into the mitochondria.<br /> | |
| - | + | * '''CPT I''' is a membrane protein which substitutes the CoA in the long-chain fatty acids by carnitine. After entering the mitochondria.<br /> | |
| - | + | * '''CPT II''' exchanges the carnitine by CoA, enabling the oxidation of the long-chain fatty acids.<ref>PMID:15363638</ref> | |
| - | + | ||
| - | + | See also [[Beta oxidation]]. | |
| - | '''Carnitine palmitoyltransferase''' (CPT I and CPT II) are involved in the transport of long-chain fatty acids into the mitochondria where they are oxidized. Fatty acids form a conjugate with CoA before being oxidized in the mitochondria. However, the CoA-long-chain fatty acid conjugates can not diffuse into the mitochondria. '''CPT I''' is a membrane protein which substitutes the CoA in the long-chain fatty acids by carnitine. After entering the mitochondria | + | |
==Disease == | ==Disease == | ||
| - | CPT I deficiency prevents the body from using certain fats for energy, particularly during fasting. | + | CPT I deficiency prevents the body from using certain fats for energy, particularly during fasting. It is associated with encephalopathy, seizures and unexpected infancy death. CPT I is important in fatty acid disorders like diabetes. |
| + | == Structural highlights == | ||
| + | |||
| + | <scene name='48/485614/Cv/11'>Substrate analog interacts with CPT II</scene> ([[2rcu]]) in a <scene name='48/485614/Cv/8'>large tunnel</scene> with its <scene name='48/485614/Cv/9'>hydrophilic head group</scene> situated at the tunnel center and the <scene name='48/485614/Cv/10'>alkyl part occupying the hydrophobic part</scene> of the tunnel. <ref>PMID:17585909</ref> | ||
| + | </StructureSection> | ||
==3D structures of carnitine palmitoyltransferase== | ==3D structures of carnitine palmitoyltransferase== | ||
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| + | [[2le3]] – hCPT I regulatory domain – human - NMR<br /> | ||
| + | [[2m76]] - hCPT I regulatory domain – NMR<br /> | ||
[[2h4t]], [[2fyo]], [[2deb]] – rCPT II – rat<br /> | [[2h4t]], [[2fyo]], [[2deb]] – rCPT II – rat<br /> | ||
[[2fw3]] - rCPT II + antidiabetic drug<br /> | [[2fw3]] - rCPT II + antidiabetic drug<br /> | ||
[[2rcu]] – rCPT II + substrate analog<br /> | [[2rcu]] – rCPT II + substrate analog<br /> | ||
[[4ep9]], [[4eph]], [[4eyw]] - rCPT II + inhibitor<br /> | [[4ep9]], [[4eph]], [[4eyw]] - rCPT II + inhibitor<br /> | ||
| - | [[2le3]] – hCPT I regulatory domain – human - NMR<br /> | ||
| - | [[2m76]] - hCPT I regulatory domain – NMR<br /> | ||
| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
| |||||||||||
3D structures of carnitine palmitoyltransferase
Updated on 16-January-2024
2le3 – hCPT I regulatory domain – human - NMR
2m76 - hCPT I regulatory domain – NMR
2h4t, 2fyo, 2deb – rCPT II – rat
2fw3 - rCPT II + antidiabetic drug
2rcu – rCPT II + substrate analog
4ep9, 4eph, 4eyw - rCPT II + inhibitor
References
- ↑ Bonnefont JP, Djouadi F, Prip-Buus C, Gobin S, Munnich A, Bastin J. Carnitine palmitoyltransferases 1 and 2: biochemical, molecular and medical aspects. Mol Aspects Med. 2004 Oct-Dec;25(5-6):495-520. PMID:15363638 doi:http://dx.doi.org/10.1016/j.mam.2004.06.004
- ↑ Rufer AC, Lomize A, Benz J, Chomienne O, Thoma R, Hennig M. Carnitine palmitoyltransferase 2: analysis of membrane association and complex structure with a substrate analog. FEBS Lett. 2007 Jul 10;581(17):3247-52. Epub 2007 Jun 8. PMID:17585909 doi:10.1016/j.febslet.2007.05.080
