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1. Techno-organisational factors of eHealth acceptance: a system dynamics model

Author

Fanta, Getnet B., Pretorius, Leon, and Erasmus, Louwrence D.

Abstract

The sustained use of eHealth is influenced by the dynamic and nonlinear interactions of technological, social, organisational and economic factors. However, most eHealth implementation frameworks are modelled linearly without capturing the complex relationship among elements of the ecosystem to ensure technology acceptance. The model-based theory-building research approach followed in this study aimed at enhancing the understanding of techno-organisational factors' influence on the acceptance of eHealth technology. A qualitative research approach and system dynamics modelling are applied to develop a system dynamic model of techno-organisational factors of eHealth acceptance. The 'average workforce turnover' showed a stronger influence on the simulated 'acceptance rate' of both eHMIS and SmartCare systems in the techno-organisational dimension. Therefore, retaining skilled workforces in the healthcare organisation should be the focus in the techno-organisational dimension of sustainable eHealth implementation to increase the 'acceptance rate' of eHMIS and SmartCare in Ethiopia.

Published
2022
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2. Structural enzymology comparisons of multifunctional enzyme, type-1 ( MFE1): the flexibility of its dehydrogenase part.

Author

Kasaragod, Prasad, Midekessa, Getnet B., Sridhar, Shruthi, Schmitz, Werner, Kiema, Tiila‐Riikka, Hiltunen, Jukka K., and Wierenga, Rik K.

Subjects
ENZYMOLOGY, MOLECULAR structure, DEHYDROGENASES, ENOYL-CoA hydratase, BINDING sites
Abstract

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. Database Structural data are available in PDB database under the accession number . [ABSTRACT FROM AUTHOR]

Published
2017
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