Functional characterization of aconitase X as a cis-3-hydroxy-L-proline dehydratase

Seiya Watanabe, Kunihiko Tajima, Satoshi Fujii, Fumiyasu Fukumori, Ryotaro Hara, Rio Fukuda, Mao Miyazaki, Kuniki Kino, Yasuo Watanabe

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Abstract

In the aconitase superfamily, which includes the archetypical aconitase, homoaconitase, and isopropylmalate isomerase, only aconitase X is not functionally annotated. The corresponding gene (LhpI) was often located within the bacterial gene cluster involved in L-hydroxyproline metabolism. Screening of a library of (hydroxy)proline analogues revealed that this protein catalyzes the dehydration of cis-3-hydroxy-L-proline to " 1 -pyrroline-2-carboxylate. Furthermore, electron paramagnetic resonance and site-directed mutagenic analyses suggests the presence of a mononuclear Fe(III) center, which may be coordinated with one glutamate and two cysteine residues. These properties were significantly different from those of other aconitase members, which catalyze the isomerization of α- to β-hydroxy acids, and have a [4Fe-4S] cluster-binding site composed of three cysteine residues. Bacteria with the LhpI gene could degrade cis-3-hydroxy-L-proline as the sole carbon source, and LhpI transcription was up-regulated not only by cis-3-hydroxy-L-proline, but also by several isomeric 3- and 4-hydroxyprolines.

Original languageEnglish
Article number38720
JournalScientific reports
Volume6
DOIs
Publication statusPublished - 2016 Dec 8

ASJC Scopus subject areas

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    Watanabe, S., Tajima, K., Fujii, S., Fukumori, F., Hara, R., Fukuda, R., Miyazaki, M., Kino, K., & Watanabe, Y. (2016). Functional characterization of aconitase X as a cis-3-hydroxy-L-proline dehydratase. Scientific reports, 6, [38720]. https://doi.org/10.1038/srep38720