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Peroxisomal multifunctional enzyme type 2 from the fruitfly: dehydrogenase and hydratase act as separate entities, as revealed by structure and kinetics.

Haataja TJ, Koski MK, Hiltunen JK, Glumoff T
Biochem J 435 771-81 (2011)
Cited: 20 times
EuropePMC logo PMID: 21320074

Abstract

All of the peroxisomal β-oxidation pathways characterized thus far house at least one MFE (multifunctional enzyme) catalysing two out of four reactions of the spiral. MFE type 2 proteins from various species display great variation in domain composition and predicted substrate preference. The gene CG3415 encodes for Drosophila melanogaster MFE-2 (DmMFE-2), complements the Saccharomyces cerevisiae MFE-2 deletion strain, and the recombinant protein displays both MFE-2 enzymatic activities in vitro. The resolved crystal structure is the first one for a full-length MFE-2 revealing the assembly of domains, and the data can also be transferred to structure-function studies for other MFE-2 proteins. The structure explains the necessity of dimerization. The lack of substrate channelling is proposed based on both the structural features, as well as by the fact that hydration and dehydrogenation activities of MFE-2, if produced as separate enzymes, are equally efficient in catalysis as the full-length MFE-2.

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  3. Stereochemistry of enzymatic water addition to C=C bonds. Chen BS, Otten LG, Hanefeld U. Biotechnol Adv 33 526-546 (2015)
  4. Caenorhabditis elegans as a model for obesity research. Yue Y, Li S, Shen P, Park Y. Curr Res Food Sci 4 692-697 (2021)
  5. Rosy Beginnings: Studying Peroxisomes in Drosophila. Pridie C, Ueda K, Simmonds AJ. Front Cell Dev Biol 8 835 (2020)

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  1. Comparative metabolomics reveals biogenesis of ascarosides, a modular library of small-molecule signals in C. elegans. von Reuss SH, Bose N, Srinivasan J, Yim JJ, Judkins JC, Sternberg PW, Schroeder FC. J Am Chem Soc 134 1817-1824 (2012)
  2. Insights into mitochondrial fatty acid synthesis from the structure of heterotetrameric 3-ketoacyl-ACP reductase/3R-hydroxyacyl-CoA dehydrogenase. Venkatesan R, Sah-Teli SK, Awoniyi LO, Jiang G, Prus P, Kastaniotis AJ, Hiltunen JK, Wierenga RK, Chen Z. Nat Commun 5 4805 (2014)
  3. Use of slow glucose feeding as supporting carbon source in lactose autoinduction medium improves the robustness of protein expression at different aeration conditions. Ukkonen K, Mayer S, Vasala A, Neubauer P. Protein Expr Purif 91 147-154 (2013)
  4. The budding yeast Pex5p receptor directs Fox2p and Cta1p into peroxisomes via its N-terminal region near the FxxxW domain. Rymer Ł, Kempiński B, Chełstowska A, Skoneczny M. J Cell Sci 131 jcs216986 (2018)
  5. The isomerase and hydratase reaction mechanism of the crotonase active site of the multifunctional enzyme (type-1), as deduced from structures of complexes with 3S-hydroxy-acyl-CoA. Kasaragod P, Schmitz W, Hiltunen JK, Wierenga RK. FEBS J 280 3160-3175 (2013)
  6. Human Δ³,Δ²-enoyl-CoA isomerase, type 2: a structural enzymology study on the catalytic role of its ACBP domain and helix-10. Onwukwe GU, Kursula P, Koski MK, Schmitz W, Wierenga RK. FEBS J 282 746-768 (2015)
  7. On the molecular basis of D-bifunctional protein deficiency type III. Mehtälä ML, Lensink MF, Pietikäinen LP, Hiltunen JK, Glumoff T. PLoS One 8 e53688 (2013)
  8. Molecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway. Sathyanarayanan N, Cannone G, Gakhar L, Katagihallimath N, Sowdhamini R, Ramaswamy S, Vinothkumar KR. Nat Commun 10 4127 (2019)
  9. Quaternary structure of human, Drosophila melanogaster and Caenorhabditis elegans MFE-2 in solution from synchrotron small-angle X-ray scattering. Mehtälä ML, Haataja TJ, Blanchet CE, Hiltunen JK, Svergun DI, Glumoff T. FEBS Lett 587 305-310 (2013)
  10. Structures of yeast peroxisomal Δ(3),Δ(2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks for the reactivity of the catalytic base and the oxyanion hole. Onwukwe GU, Koski MK, Pihko P, Schmitz W, Wierenga RK. Acta Crystallogr D Biol Crystallogr 71 2178-2191 (2015)
  11. Biallelic mutation of HSD17B4 induces middle age-onset spinocerebellar ataxia. Matsuda Y, Morino H, Miyamoto R, Kurashige T, Kume K, Mizuno N, Kanaya Y, Tada Y, Ohsawa R, Yokota K, Shimozawa N, Maruyama H, Kawakami H. Neurol Genet 6 e396 (2020)
  12. Sequence analysis and structure prediction of enoyl-CoA hydratase from Avicennia marina: implication of various amino acid residues on substrate-enzyme interactions. Jabeen U, Salim A. Phytochemistry 94 36-44 (2013)


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