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The roles of diol dehydratase from pdu operon on glycerol catabolism in Klebsiella pneumoniae

Shu, L; Wang, Q; Jiang, W; Tišma, M; Oh, B; Shi, J; Lye, GJ; ... Hao, J; + view all (2022) The roles of diol dehydratase from pdu operon on glycerol catabolism in Klebsiella pneumoniae. Enzyme and Microbial Technology , 157 , Article 110021. 10.1016/j.enzmictec.2022.110021. Green open access

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Abstract

The dha operon of Klebsiella pneumoniae is responsible for glycerol catabolism and 1,3-propanediol formation. Subunits of glycerol dehydratase and the large subunit of glycerol dehydratase reactivating factor are encoded by dhaBCE and dhaF, respectively. Proteins of pdu operon form a microcompartment (bacteria organelle) and responsible for 1,2-propanediol catabolism. In this operon, pduCDE and pduG encode subunits of diol dehydratase and its reactivating factor. Diol dehydratase is an isofunctional enzyme of glycerol dehydratase, but its role in glycerol catabolism was not entirely clear. In this study, dhaBCE, pduCDE, dhaF, and pduG in K. pneumoniae were knocked out individually or combinedly. These strains were cultured with glycerol as a substrate, and dehydratase activities in the cytoplasm and microcompartment were detected. Results showed that glycerol dehydratase and diol dehydratase were simultaneously responsible for glycerol catabolism in K. pneumoniae. Besides being packaged in microcompartment, large amounts of diol dehydratase was also presented in the cytoplasm. However, the Pdu microcompartment reduced the accumulation of 3-hydroxypropionaldehyde in the fermentation broth. PduG can cross reactivate glycerol dehydratase instead of DhaF. However, DhaF is not involved in reactivation of diol dehydratase. In conclusion, diol dehydratase and Pdu microcompartment play important roles in glycerol catabolism in K. pneumoniae.

Type: Article
Title: The roles of diol dehydratase from pdu operon on glycerol catabolism in Klebsiella pneumoniae
Location: United States
Open access status: An open access version is available from UCL Discovery
DOI: 10.1016/j.enzmictec.2022.110021
Publisher version: https://doi.org/10.1016/j.enzmictec.2022.110021
Language: English
Additional information: This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions.
Keywords: 1,3-propanediol, Diol dehydratase, Glycerol dehydratase, Klebsiella pneumoniae, Microcompartment, Cobamides, Glycerol, Hydro-Lyases, Klebsiella pneumoniae, Operon, Propanediol Dehydratase
UCL classification: UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Engineering Science
UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Engineering Science > Dept of Biochemical Engineering
UCL > Provost and Vice Provost Offices > UCL BEAMS
UCL
URI: https://discovery.ucl.ac.uk/id/eprint/10148078
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