A novel meta-cleavage product hydrolase from Flavobacterium sp. ATCC27551

Biochem Biophys Res Commun. 2006 Dec 22;351(3):675-81. doi: 10.1016/j.bbrc.2006.10.080. Epub 2006 Oct 24.

Abstract

The organophosphate degrading (opd) gene cluster of plasmid pPDL2 of Flavobacterium sp. ATCC27551 contains a novel open-reading frame, orf243. This was predicted to encode an alpha/beta hydrolase distantly related to the meta-fission product (MFP) hydrolases such as XylF, PhnD, and CumD. By homology modeling Orf243 has most of the structural features of MFP hydrolases including the characteristic active site catalytic triad. The purified protein (designated MfhA) is a homotetramer and shows similar affinity for 2-hydroxy-6-oxohepta-2,4-dienoate (HOHD), 2-hydroxymuconic semialdehyde (HMSA), and 2-hydroxy-5-methylmuconic semialdehyde (HMMSA), the meta-fission products of 3-methyl catechol, catechol, and 4-methyl catechol. The unique catalytic properties of MfhA and the presence near its structural gene of cis-elements required for transposition suggest that mfhA has evolved towards encoding a common hydrolase that can act on meta-fission products containing either aldehyde or ketone groups.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Catalysis
  • Computer Simulation
  • Enzyme Activation
  • Flavobacterium / enzymology*
  • Flavobacterium / genetics*
  • Hydrolases / chemistry*
  • Hydrolases / genetics*
  • Models, Chemical*
  • Models, Molecular*
  • Molecular Sequence Data
  • Protein Binding
  • Protein Conformation

Substances

  • Hydrolases