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

操纵子 甘油 脱水酶 分解代谢 肺炎克雷伯菌 生物化学 生物 细菌 微生物学 大肠杆菌 遗传学 基因
作者
Lin Shu,Qinghui Wang,Weiyan Jiang,Marina Tišma,Beak-Rock Oh,Jiping Shi,Gary J. Lye,Frank Baganz,Dong Wei,Jian Hao
出处
期刊:Enzyme and microbial technology [Elsevier]
卷期号:157: 110021-110021 被引量:8
标识
DOI:10.1016/j.enzmictec.2022.110021
摘要

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.
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