TY  - JOUR
A1  - Kasaragod, Prasad
A1  - Midekessa, Getnet B.
A1  - Sridhar, Shruthi
A1  - Schmitz, Werner
A1  - Kiema, Tiila-Riikka
A1  - Hiltunen, Jukka K.
A1  - Wierenga, Rik K.
T1  - Structural enzymology comparisons of multifunctional enzyme, type-1 (MFE1): the flexibility of its dehydrogenase part
JF  - FEBS Open Bio
N2  - 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.
KW  - biology
KW  - CoA
KW  - crotonase
KW  - dehydrogenase
KW  - NAD
KW  - substrate channeling
Y1  - 2017
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-172732
VL  - 7
IS  - 12
ER  -