Kasaragod, P., Midekessa, G.B., Sridhar, S., Schmitz, W., Kiema, T.-R., Hiltunen, J.K. and Wierenga, R.K. (2017), Structural enzymology comparisons of multifunctional enzyme, type-1 (MFE1): the flexibility of its dehydrogenase part. FEBS Open Bio, 7: 1830-1842. https://doi.org/10.1002/2211-5463.12337
Structural enzymology comparisons of multifunctional enzyme, type‐1 (MFE1) : the flexibility of its dehydrogenase part
|Author:||Kasaragod, Prasad1; Midekessa, Getnet B.1; Sridhar, Shruthi1;|
1University of Oulu Biocenter Oulu and Faculty of Biochemistry and Molecular Medicine Finland
2University of Würzburg Theodor Boveri Institute of Biosciences (Biocenter) Germany
|Online Access:||PDF Full Text (PDF, 1.1 MB)|
|Persistent link:|| http://urn.fi/urn:nbn:fi-fe2019050314191
John Wiley & Sons,
|Publish Date:|| 2019-05-03
Multifunctional enzyme, type‐1 (MFE1) is a monomeric enzyme with a 2E‐enoyl‐CoA hydratase and a 3S‐hydroxyacyl‐CoA dehydrogenase (HAD) active site. Enzyme kinetic data of rat peroxisomal MFE1 show that the catalytic efficiencies for converting the short‐chain substrate 2E‐butenoyl‐CoA into acetoacetyl‐CoA are much lower when compared with those of the homologous monofunctional enzymes. The mode of binding of acetoacetyl‐CoA (to the hydratase active site) and the very similar mode of binding of NAD+ and NADH (to the HAD part) are described and compared with those of their monofunctional counterparts. Structural comparisons suggest that the conformational flexibility of the HAD and hydratase parts of MFE1 are correlated. The possible importance of the conformational flexibility of MFE1 for its biocatalytic properties is discussed.
FEBS open bio
|Pages:||1830 - 1842|
|Type of Publication:||
A1 Journal article – refereed
|Field of Science:||
1182 Biochemistry, cell and molecular biology
The support of a Biocenter Finland Grant to RKW is gratefully acknowledged.
Additional Supporting Information may be found online in the supporting information tab for this article.
Structural data are available in PDB database under the accession number 5MGB.
© 2017 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.