Low-solubility glycerol dehydratase, a chimeric enzyme of coenzyme B 12-dependent glycerol and diol dehydratases

Takamasa Tobimatsu, Tsuneo Nishiki, Masaya Morimoto, Ryou Miyata, Tetsuo Toraya

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Coenzyme B12-dependent diol and glycerol dehydratases are isofunctional enzymes, which catalyze dehydration of 1, 2-diols to produce corresponding aldehydes. Although the two types of dehydratases have high sequence homology, glycerol dehydratase is a soluble cytosolic enzyme, whereas diol dehydratase is a low-solubility enzyme associated with carboxysome-like polyhedral organelles. Since both the N-terminal 20 and 16 amino acid residues of the β and γ subunits, respectively, are indispensable for the low solubility of diol dehydratase, we constructed glycerol dehydratase-based chimeric enzymes which carried N-terminal portions of the β and γ subunits of diol dehydratase in the corresponding subunits of glycerol dehydratase. Addition of the diol dehydratase-specific N-terminal 34 and 33 amino acid residues of the β and γ subunits, respectively, was not enough to lower the solubility of glycerol dehydratase. A chimeric enzyme which carries the low homology region (residues 35-60) of the diol dehydratase β subunit in addition to the diol dehydratase-specific extra-regions of β and γ subunits showed low solubility comparable to diol dehydratase, although its hydropathy plot does not show any prominent hydrophobic peaks in these regions. It was thus concluded that short N-terminal sequences are sufficient to change the solubility of the enzyme.

Original languageEnglish
Pages (from-to)199-206
Number of pages8
JournalArchives of Microbiology
Volume191
Issue number3
DOIs
Publication statusPublished - Mar 2009

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Keywords

  • Chimeric enzyme
  • Coenzyme B
  • Diol dehydratase
  • Glycerol dehydratase
  • Low solubility

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Biochemistry
  • Genetics

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