1.3.8.7: medium-chain acyl-CoA dehydrogenase

This is an abbreviated version!
For detailed information about medium-chain acyl-CoA dehydrogenase, go to the full flat file.

Word Map on EC 1.3.8.7

Reaction

a medium-chain acyl-CoA
+
electron-transfer flavoprotein
=
a medium-chain trans-2,3-dehydroacyl-CoA
+
reduced electron-transfer flavoprotein

Synonyms

ACAD-9, ACADM, ACD, acyl CoA dehydrogenase, acyl coenzyme A dehydrogenase, acyl dehydrogenase, acyl-CoA dehydrogenase, acyl-CoA dehydrogenase-9, dehydrogenase, acyl coenzyme A, EC 1.3.2.2, FadE, fatty acyl coenzyme A dehydrogenase, fatty-acyl-CoA dehydrogenase, general ACAD, general acyl CoA dehydrogenase, LCAD, LipB, MCAD, MCADH, medium chain acyl-CoA dehydrogenase, medium chain-specific acyl-CoA oxidase, medium-chain acyl CoA dehydrogenase, medium-chain acyl-CoA dehydrogenase, medium-chain acyl-coenzyme A dehydrogenase, medium-chain coenzyme A dehydrogenase, pMCAD, PP_1893, PP_2039, PP_2048, PP_2437

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.8 With a flavin as acceptor
                1.3.8.7 medium-chain acyl-CoA dehydrogenase

Crystallization

Crystallization on EC 1.3.8.7 - medium-chain acyl-CoA dehydrogenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
molecular dynamics simulation and comparison between the porcine MCAD and human MCAD structures. Both proteins are essentially similar
-
wild-type and E376G/T255E double mutant enzyme and enzyme substrate complexes, vapor diffusion method at 4°C using the sitting drop technique, 0.027 mg enzyme in 140 mM Tris-acetate, pH 7.0, 8% w/v polyethylene glycol 4000, the human enzyme structure is essentially the same as that of the pig enzyme
-
5-10 mg/ml enzyme in 50 mM potassium phosphate, pH 7.5, 0.1 mM EDTA, 2% polyethylene glycol 6000, 4°C, after 7 days 5% polyethylene glycol, crystals emerge 2-3 days later
-
dialysis against distilled water at 4°C
-
FT-IR spectroscopic studies. The hydrogen-bond enthalpy change responsible for the polarization on the transfer of the substrate from aqueous solution to the active site of enzyme is estimated to be 15 kcal/mol. The 1626 per cm band is noticeably weakened in the case of acyl-CoA with acyl chains longer than C12 which are poor substrates, suggesting that C(1) =O is likely to exist in multiple orientations in the active-site cavity, whence the band becomes obscured. A band identical to that of bound C8-CoA is observed in the case of C4-CoA which is a poor substrate, indicating the strong hydrogen bond at C(1)-O
-
molecular dynamics simulation and comparison between the porcine MCAD and human MCAD structures. Both proteins are essentially similar
sitting-drop method, native enzyme and enzyme-substrate complex, x-ray structure, 2.4 A resolution, monomer is folded into 3 domains of approx. equal size, the flavin ring is located in a crevice between the beta-domain and the C-terminal domain
-
x-ray structure, 3.0 A resolution
-