CATH Classification

Domain Context

CATH Clusters

Superfamily Butyryl-CoA Dehydrogenase, subunit A, domain 3
Functional Family very long-chain specific acyl-CoA dehydrogenase, mitochondrial

Enzyme Information

1.3.8.9
Very-long-chain acyl-CoA dehydrogenase.
based on mapping to UniProt P49748
A very-long-chain acyl-CoA + electron-transfer flavoprotein = a very- long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.
-!- One of several enzymes that catalyze the first step in fatty acids beta-oxidation. -!- The enzyme is most active toward long-chain acyl-CoAs such as C(14), C(16) and C(18), but is also active with very-long-chain acyl-CoAs up to 24 carbons. -!- It shows no activity for substrates of less than 12 carbons. -!- It's specific activity toward palmitoyl-CoA is more than 10-fold that of the long-chain acyl-CoA dehydrogenase. -!- cf. EC 1.3.8.1, EC 1.3.8.7 and EC 1.3.8.8. -!- Formerly EC 1.3.99.3.

UniProtKB Entries (1)

P49748
ACADV_HUMAN
Homo sapiens
Very long-chain specific acyl-CoA dehydrogenase, mitochondrial

PDB Structure

PDB 3B96
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase.
McAndrew, R.P., Wang, Y., Mohsen, A.W., He, M., Vockley, J., Kim, J.J.
J.Biol.Chem.