Identification of the in vivo function of the high-efficiency d -mannonate dehydratase in caulobacter crescentus NA1000 from the enolase superfamily

Daniel J. Wichelecki; Dylan C. Graff; Nawar Al-Obaidi; Steven C. Almo; John A. Gerlt

doi:10.1021/bi500683x

Identification of the in vivo function of the high-efficiency d -mannonate dehydratase in caulobacter crescentus NA1000 from the enolase superfamily

Daniel J. Wichelecki, Dylan C. Graff, Nawar Al-Obaidi, Steven C. Almo, John A. Gerlt

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Abstract

The d-mannonate dehydratase (ManD) subgroup of the enolase superfamily contains members with varying catalytic activities (high-efficiency, low-efficiency, or no activity) that dehydrate d-mannonate and/or d-gluconate to 2-keto-3-deoxy-d-gluconate [Wichelecki, D. J., et al. (2014) Biochemistry 53, 2722-2731]. Despite extensive in vitro characterization, the in vivo physiological role of a ManD has yet to be established. In this study, we report the in vivo functional characterization of a high-efficiency ManD from Caulobacter crescentus NA1000 (UniProt entry B8GZZ7) by in vivo discovery of its essential role in d-glucuronate metabolism. This in vivo functional annotation may be extended to ∼50 additional proteins.

Original language	English (US)
Pages (from-to)	4087-4089
Number of pages	3
Journal	Biochemistry
Volume	53
Issue number	25
DOIs	https://doi.org/10.1021/bi500683x
State	Published - Jul 1 2014

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Biochemistry

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title = "Identification of the in vivo function of the high-efficiency d -mannonate dehydratase in caulobacter crescentus NA1000 from the enolase superfamily",

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AU - Wichelecki, Daniel J.

AU - Graff, Dylan C.

AU - Al-Obaidi, Nawar

AU - Almo, Steven C.

AU - Gerlt, John A.

PY - 2014/7/1

Y1 - 2014/7/1

N2 - The d-mannonate dehydratase (ManD) subgroup of the enolase superfamily contains members with varying catalytic activities (high-efficiency, low-efficiency, or no activity) that dehydrate d-mannonate and/or d-gluconate to 2-keto-3-deoxy-d-gluconate [Wichelecki, D. J., et al. (2014) Biochemistry 53, 2722-2731]. Despite extensive in vitro characterization, the in vivo physiological role of a ManD has yet to be established. In this study, we report the in vivo functional characterization of a high-efficiency ManD from Caulobacter crescentus NA1000 (UniProt entry B8GZZ7) by in vivo discovery of its essential role in d-glucuronate metabolism. This in vivo functional annotation may be extended to ∼50 additional proteins.

AB - The d-mannonate dehydratase (ManD) subgroup of the enolase superfamily contains members with varying catalytic activities (high-efficiency, low-efficiency, or no activity) that dehydrate d-mannonate and/or d-gluconate to 2-keto-3-deoxy-d-gluconate [Wichelecki, D. J., et al. (2014) Biochemistry 53, 2722-2731]. Despite extensive in vitro characterization, the in vivo physiological role of a ManD has yet to be established. In this study, we report the in vivo functional characterization of a high-efficiency ManD from Caulobacter crescentus NA1000 (UniProt entry B8GZZ7) by in vivo discovery of its essential role in d-glucuronate metabolism. This in vivo functional annotation may be extended to ∼50 additional proteins.

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Identification of the in vivo function of the high-efficiency d -mannonate dehydratase in caulobacter crescentus NA1000 from the enolase superfamily

Abstract

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