Skip to main content
European Commission logo
Deutsch Deutsch
CORDIS - Forschungsergebnisse der EU
CORDIS
CORDIS Web 30th anniversary CORDIS Web 30th anniversary

Structural and biochemical studies of an ancestral enzyme with dual dehalogenase and luciferase activity

Ziel

Haloalkane dehalogenases (HLDs) catalyse the cleavage of the carbon-halogen bond of industrial organohalogen compounds and are interesting subjects to study molecular evolution. Strikingly, HLDs display remarkable sequence and structural similarity with luciferase from the marine invertebrate Renilla reniformis (RLuc), which reflects their common evolutionary history. Unlike HLDs, which are α/β hydrolases (EC 3.8.1.5) the RLuc luciferase is cofactor-independent monooxygenase (EC 1.13.12.5) that converts coelenterazine into coelenteramide and carbon dioxide, followed by an emission of blue light. Yet, the evolutionary steps driving their functional divergence remain poorly understood. Our proof-of-concept data show the feasibility of the reconstruction of an ancestral enzyme, which existed prior to the functional divergence of the modern-day HLD and RLuc homologues, and that this in-lab resurrected enzyme exhibits so-far unobserved dual dehalogenase/luciferase activity. This project aims to dissect structural and biochemical basis of this unusual biocatalytic behaviour of the ancestral enzyme. Specifically, X-ray crystallography, including time-resolved studies with photo-switchable substrate analogues, and advanced mass spectrometry techniques will be employed to probe enzyme-substrate complexes in order to get molecular insights into the inner organization and workings of the catalytically promiscuous enzyme. Complementary site-directed mutagenesis and molecular dynamics simulations will explore the contributions of individual amino acid residues to the dual-function activity. The gained knowledge will extend our in-depth understanding of the evolution of underlying biocatalytic reaction mechanisms. Furthermore, it will pave the way for the development of novel software tools for the rational engineering of next-generation biocatalysts for specific uses in biotechnology and biomedicine.

Wissenschaftliches Gebiet (EuroSciVoc)

CORDIS klassifiziert Projekte mit EuroSciVoc, einer mehrsprachigen Taxonomie der Wissenschaftsbereiche, durch einen halbautomatischen Prozess, der auf Verfahren der Verarbeitung natürlicher Sprache beruht.

Sie müssen sich anmelden oder registrieren, um diese Funktion zu nutzen

Koordinator

Masarykova univerzita
Netto-EU-Beitrag
€ 142 720,80
Adresse
Zerotinovo namesti 9
601 77 Brno
Tschechien

Auf der Karte ansehen

Region
Česko Jihovýchod Jihomoravský kraj
Aktivitätstyp
Higher or Secondary Education Establishments
Links
Gesamtkosten
€ 142 720,80