Discovery of an L-fucono-1,5-lactonase from cog3618 of the amidohydrolase superfamily

Biochemistry. 2013 Jan 8;52(1):239-53. doi: 10.1021/bi3015554. Epub 2012 Dec 20.


A member of the amidohydrolase superfamily, BmulJ_04915 from Burkholderia multivorans, of unknown function was determined to hydrolyze a series of sugar lactones: L-fucono-1,4-lactone, D-arabino-1,4-lactone, L-xylono-1,4-lactone, D-lyxono-1,4-lactone, and L-galactono-1,4-lactone. The highest activity was shown for L-fucono-1,4-lactone with a k(cat) value of 140 s(-1) and a k(cat)/K(m) value of 1.0 × 10(5) M(-1) s(-1) at pH 8.3. The enzymatic product of an adjacent L-fucose dehydrogenase, BmulJ_04919, was shown to be L-fucono-1,5-lactone via nuclear magnetic resonance spectroscopy. L-Fucono-1,5-lactone is unstable and rapidly converts nonenzymatically to L-fucono-1,4-lactone. Because of the chemical instability of L-fucono-1,5-lactone, 4-deoxy-L-fucono-1,5-lactone was enzymatically synthesized from 4-deoxy-L-fucose using L-fucose dehydrogenase. BmulJ_04915 hydrolyzed 4-deoxy-L-fucono-1,5-lactone with a k(cat) value of 990 s(-1) and a k(cat)/K(m) value of 8.0 × 10(6) M(-1) s(-1) at pH 7.1. The protein does not require divalent cations in the active site for catalytic activity. BmulJ_04915 is the second enzyme from cog3618 of the amidohydrolase superfamily that does not require a divalent metal for catalytic activity. BmulJ_04915 is the first enzyme that has been shown to catalyze the hydrolysis of either L-fucono-1,4-lactone or L-fucono-1,5-lactone. The structures of the fuconolactonase and the fucose dehydrogenase were determined by X-ray diffraction methods.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amidohydrolases / chemistry*
  • Amidohydrolases / metabolism*
  • Burkholderia / chemistry
  • Burkholderia / enzymology*
  • Burkholderia / metabolism
  • Carbohydrate Dehydrogenases / chemistry
  • Carbohydrate Dehydrogenases / metabolism
  • Catalytic Domain
  • Crystallography, X-Ray
  • Fucose / metabolism*
  • Hydrolysis
  • Lactones / metabolism*
  • Models, Molecular
  • NADP / metabolism
  • Protein Conformation
  • Substrate Specificity
  • Sugar Acids / metabolism


  • Lactones
  • Sugar Acids
  • galactono-1,4-lactone
  • Fucose
  • L-arabino-1,4-lactone
  • NADP
  • Carbohydrate Dehydrogenases
  • L-fucose dehydrogenase
  • Amidohydrolases

Associated data

  • PDB/4DLF
  • PDB/4DLM
  • PDB/4DNM
  • PDB/4DO7
  • PDB/4GKB
  • PDB/4GLO
  • PDB/4GVX