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Characterization of Multifunctional Enzyme Complexes from Comamonas testosteroni KF1 and Thermomonospora curvata DSM 43183 Involved in Steroid Side Chain Degradation

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Title: Characterization of Multifunctional Enzyme Complexes from Comamonas testosteroni KF1 and Thermomonospora curvata DSM 43183 Involved in Steroid Side Chain Degradation
Author: Aggett, Rebecca
Department: Department of Molecular and Cellular Biology
Program: Molecular and Cellular Biology
Advisor: Seah, Stephen
Abstract: The genes fadI and fadJ from Comamonas testosteroni KF1 are homologous to genes encoding the components of multifunctional enzyme complexes involved in fatty acid side chain β-oxidation. Both of these genes are located within the steroid degradation locus in the genome. FadJ had hydratase activity towards the 5-carbon side chain of cholic acid metabolite; however, gene knockout studies revealed no phenotypic changes in growth patterns. In the Actinobacterium Thermomonospora curvata DSM 43183, the genes Tcur3480, Tcur3482 and ltp2Tcur, located within a steroid side chain degrading operon, together encode a multifunctional steroid degrading enzyme complex. It was previously determined that the aldolase Ltp2Tcur associates with the hydratase Tcur3480-Tcur3482 through the DUF35 domain, although the catalytic mechanism and kinetic parameters were unknown. The crystal structure of Ltp2Tcur-DUF35 was solved and wild-type and mutant variant kinetic parameters were determined to support a proposed, novel retro-aldol catalytic mechanism involving two catalytic tyrosine residues.
URI: http://hdl.handle.net/10214/14655
Date: 2018-11
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