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| Home > Publications database > Crystal structures of apo- and FAD-bound human peroxisomal acyl-CoA oxidase provide mechanistic basis explaining clinical observations > print |
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| 024 | 7 | _ | |a 10.1016/j.ijbiomac.2022.02.008 |2 doi |
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| 100 | 1 | _ | |a Sonani, Ravi R. |b 0 |
| 245 | _ | _ | |a Crystal structures of apo- and FAD-bound human peroxisomal acyl-CoA oxidase provide mechanistic basis explaining clinical observations |
| 260 | _ | _ | |a New York, NY [u.a.] |c 2022 |b Elsevier |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 520 | _ | _ | |a Peroxisomal acyl-CoA oxidase 1a (ACOX1a) catalyzes the first and rate-limiting step of fatty acid oxidation, the conversion of acyl-CoAs to 2-trans-enoyl-CoAs. The dysfunction of human ACOX1a (hACOX1a) leads to deterioration of the nervous system manifesting in myeloneuropathy, hypotonia and convulsions. Crystal structures of hACOX1a in apo- and cofactor (FAD)-bound forms were solved at 2.00 and 2.09 Å resolution, respectively. hACOX1a exists as a homo-dimer with solvation free energy gain (ΔGo) of −44.7 kcal mol−1. Two FAD molecules bind at the interface of protein monomers completing the active sites. The substrate binding cleft of hACOX1a is wider compared to human mitochondrial very-long chain specific acyl-CoA dehydrogenase. Mutations (p.G178C, p.M278V and p.N237S) reported to cause dysfunctionality of hACOX1a are analyzed on its 3D-structure to understand structure-function related perturbations and explain the associated phenotypes. |
| 536 | _ | _ | |a 6G3 - PETRA III (DESY) (POF4-6G3) |0 G:(DE-HGF)POF4-6G3 |c POF4-6G3 |f POF IV |x 0 |
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| 700 | 1 | _ | |a Blat, Artur |b 1 |
| 700 | 1 | _ | |a Dubin, Grzegorz |0 P:(DE-H253)PIP1021406 |b 2 |e Corresponding author |
| 773 | _ | _ | |a 10.1016/j.ijbiomac.2022.02.008 |g Vol. 205, p. 203 - 210 |0 PERI:(DE-600)1483284-7 |p 203 - 210 |t International journal of biological macromolecules |v 205 |y 2022 |x 0141-8130 |
| 856 | 4 | _ | |u https://www.sciencedirect.com/science/article/pii/S0141813022002434 |
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