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 Alan Gerlt

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)4087-4089
Number of pages3
JournalBiochemistry
Volume53
Issue number25
DOIs
StatePublished - Jul 1 2014

Fingerprint

Caulobacter crescentus
Phosphopyruvate Hydratase
Glucuronic Acid
Biochemistry
Metabolism
Catalyst activity
mannonate dehydratase
Proteins
gluconic acid

ASJC Scopus subject areas

  • Biochemistry

Cite this

Identification of the in vivo function of the high-efficiency d -mannonate dehydratase in caulobacter crescentus NA1000 from the enolase superfamily. / Wichelecki, Daniel J.; Graff, Dylan C.; Al-Obaidi, Nawar; Almo, Steven C.; Gerlt, John Alan.

In: Biochemistry, Vol. 53, No. 25, 01.07.2014, p. 4087-4089.

Research output: Contribution to journalArticle

Wichelecki, Daniel J. ; Graff, Dylan C. ; Al-Obaidi, Nawar ; Almo, Steven C. ; Gerlt, John Alan. / Identification of the in vivo function of the high-efficiency d -mannonate dehydratase in caulobacter crescentus NA1000 from the enolase superfamily. In: Biochemistry. 2014 ; Vol. 53, No. 25. pp. 4087-4089.
@article{43ccebe100794cffbb8926577396f6c7,
title = "Identification of the in vivo function of the high-efficiency d -mannonate dehydratase in caulobacter crescentus NA1000 from the enolase superfamily",
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.",
author = "Wichelecki, {Daniel J.} and Graff, {Dylan C.} and Nawar Al-Obaidi and Almo, {Steven C.} and Gerlt, {John Alan}",
year = "2014",
month = "7",
day = "1",
doi = "10.1021/bi500683x",
language = "English (US)",
volume = "53",
pages = "4087--4089",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "25",

}

TY - JOUR

T1 - Identification of the in vivo function of the high-efficiency d -mannonate dehydratase in caulobacter crescentus NA1000 from the enolase superfamily

AU - Wichelecki, Daniel J.

AU - Graff, Dylan C.

AU - Al-Obaidi, Nawar

AU - Almo, Steven C.

AU - Gerlt, John Alan

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.

UR - http://www.scopus.com/inward/record.url?scp=84903734297&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84903734297&partnerID=8YFLogxK

U2 - 10.1021/bi500683x

DO - 10.1021/bi500683x

M3 - Article

VL - 53

SP - 4087

EP - 4089

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 25

ER -