Characterization of feedback-resistant mevalonate kinases from the methanogenic archaeons Methanosaeta concilii and Methanocella paludicola | Zendy

Ekaterina Kazieva | Zendy; Yoko Yamamoto | Zendy; Yoshinori Tajima | Zendy; K. Yokoyama | Zendy; J. I. Katashkina | Zendy; Yousuke Nishio | Zendy

Open Access

Characterization of feedback-resistant mevalonate kinases from the methanogenic archaeons Methanosaeta concilii and Methanocella paludicola

Author(s) -

Ekaterina Kazieva,

Yoko Yamamoto,

Yoshinori Tajima,

K. Yokoyama,

J. I. Katashkina,

Yousuke Nishio

Publication year - 2017

Publication title -

microbiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.019

H-Index - 179

eISSN - 1465-2080

pISSN - 1350-0872

DOI - 10.1099/mic.0.000510

Subject(s) - methanosaeta , biology , microbiology and biotechnology , chemistry , bacteria , methanogenesis , genetics

The inhibition of mevalonate kinase (MVK) by downstream metabolites is an important mechanism in the regulation of isoprenoid production in a broad range of organisms. The first feedback-resistant MVK was previously discovered in the methanogenic archaeon Methanosarcinamazei. Here, we report the cloning, expression, purification, kinetic characterization and inhibition analysis of MVKs from two other methanogens, Methanosaetaconcilii and Methanocellapaludicola. Similar to the M. mazei MVK, these enzymes were not inhibited by diphosphomevalonate (DPM), dimethylallyl diphosphate (DMAPP), isopentenyldiphosphate (IPP), geranylpyrophosphate (GPP) or farnesylpyrophosphate (FPP). However, they exhibited significantly higher affinity to mevalonate and higher catalytic efficiency than the previously characterized enzyme.

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