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

Merlin Eric Hobbs, Matthew Vetting, Howard J. Williams, Tamari Narindoshvili, Devon M. Kebodeaux, Brandan Hillerich, Ronald D. Seidel, Steven C. Almo, Frank M. Raushel

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

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 kcat value of 140 s -1 and a kcat/Km 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 kcat value of 990 s-1 and a kcat/Km value of 8.0 × 106 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.

Original languageEnglish (US)
Pages (from-to)239-253
Number of pages15
JournalBiochemistry
Volume52
Issue number1
DOIs
StatePublished - Jan 8 2013

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Amidohydrolases
Lactones
L-fucose dehydrogenase
Catalyst activity
Burkholderia
Fucose
Divalent Cations
Enzymes
X-Ray Diffraction

ASJC Scopus subject areas

  • Biochemistry

Cite this

Hobbs, M. E., Vetting, M., Williams, H. J., Narindoshvili, T., Kebodeaux, D. M., Hillerich, B., ... Raushel, F. M. (2013). Discovery of an l-fucono-1,5-lactonase from cog3618 of the amidohydrolase superfamily. Biochemistry, 52(1), 239-253. https://doi.org/10.1021/bi3015554

Discovery of an l-fucono-1,5-lactonase from cog3618 of the amidohydrolase superfamily. / Hobbs, Merlin Eric; Vetting, Matthew; Williams, Howard J.; Narindoshvili, Tamari; Kebodeaux, Devon M.; Hillerich, Brandan; Seidel, Ronald D.; Almo, Steven C.; Raushel, Frank M.

In: Biochemistry, Vol. 52, No. 1, 08.01.2013, p. 239-253.

Research output: Contribution to journalArticle

Hobbs, ME, Vetting, M, Williams, HJ, Narindoshvili, T, Kebodeaux, DM, Hillerich, B, Seidel, RD, Almo, SC & Raushel, FM 2013, 'Discovery of an l-fucono-1,5-lactonase from cog3618 of the amidohydrolase superfamily', Biochemistry, vol. 52, no. 1, pp. 239-253. https://doi.org/10.1021/bi3015554
Hobbs ME, Vetting M, Williams HJ, Narindoshvili T, Kebodeaux DM, Hillerich B et al. Discovery of an l-fucono-1,5-lactonase from cog3618 of the amidohydrolase superfamily. Biochemistry. 2013 Jan 8;52(1):239-253. https://doi.org/10.1021/bi3015554
Hobbs, Merlin Eric ; Vetting, Matthew ; Williams, Howard J. ; Narindoshvili, Tamari ; Kebodeaux, Devon M. ; Hillerich, Brandan ; Seidel, Ronald D. ; Almo, Steven C. ; Raushel, Frank M. / Discovery of an l-fucono-1,5-lactonase from cog3618 of the amidohydrolase superfamily. In: Biochemistry. 2013 ; Vol. 52, No. 1. pp. 239-253.
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abstract = "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 kcat value of 140 s -1 and a kcat/Km 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 kcat value of 990 s-1 and a kcat/Km value of 8.0 × 106 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.",
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AU - Vetting, Matthew

AU - Williams, Howard J.

AU - Narindoshvili, Tamari

AU - Kebodeaux, Devon M.

AU - Hillerich, Brandan

AU - Seidel, Ronald D.

AU - Almo, Steven C.

AU - Raushel, Frank M.

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N2 - 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 kcat value of 140 s -1 and a kcat/Km 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 kcat value of 990 s-1 and a kcat/Km value of 8.0 × 106 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.

AB - 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 kcat value of 140 s -1 and a kcat/Km 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 kcat value of 990 s-1 and a kcat/Km value of 8.0 × 106 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.

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