Acyl-CoA dehydrogenase

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{{STRUCTURE_3mde| PDB=3mde | SIZE=400| SCENE= |right|CAPTION=Pig medium chain acyl-CoA hydrogenase complex with cofactor FAD and octanoyl-CoA [[3mde]] }}
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Revision as of 09:28, 30 April 2012

Template:STRUCTURE 3mde

Acyl-CoA dehydrogenase (ACDH) catalyzes the introduction of a double bond between C2 and C3 of the thio-ester CoA substrate. This is the first reaction in fatty acid metabolism which produces acetyl-CoA. FAD is the cofactor of ACDH activity. ACDH is classified according to the length of its substrates as short- (SCAD), medium- (MCAD), very- and very long-chain (VLCAD) ACDH. Impairment of the activity of ACDH causes a variety of diseases associated with lack of fatty acid metabolism.

3D structures of acyl-CoA dehydrogenase

Short chain ACDH

1jqi - SCAD + acetoacetyl-CoA + FAD – rat
2dvl, 2z1q - TtSCAD + FAD – Thermus thermophilus
2jif, 2vig - hSCAD + CoA persulfide + FAD – human

Medium chain ACDH

1ws9, 2cx9 - TtMCAD
3mdd – pMCAD + FAD – pig
1egd, 1ege - hMCAD (mutant) + FAD
1ukw, 2d29 - TtMCAD + FAD
1egc - hMCAD (mutant) + octanoyl-CoA + FAD
3mde - pMCAD + octanoyl-CoA + FAD
1udy - pMCAD + thiaoctanoyl-CoA + FAD
1t9g - hMCAD + electron transfer flavoprotein + AMP + FAD
2a1t - hMCAD + electron transfer flavoprotein (mutant) + AMP + FAD

Very long chain ACDH

2uxw - hVLCAD + tetradecanoyl CoA + FAD
3b96 - hVLCAD + trans-δ2-palmitenoyl CoA + FAD

Unspecified ACDH

2oku – ACDH C terminal – Porphyromonas gingivalis
2pg0 - ACDH + FAD – Geobacillus kaustophilus
2wbi – hACDH 11 + FAD
3nf4, 3pfd – ACHD + FAD – Mycobacterium thermoresistibile
3owa - ACDH + FAD – Bacillus anthracis

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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