Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants

Cindy Rosenthal; Uwe Mueller; Santosh Panjikar; Lianli Sun; Martin Ruppert; Yu Zhao; Joachim Stöckigt

doi:10.1107/S174430910605041X

Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants

Cindy Rosenthal, Uwe Mueller, Santosh Panjikar, Lianli Sun, Martin Ruppert, Yu Zhao, Joachim Stöckigt

Research output: Contribution to journal › Article › Research › peer-review

15 Citations (Scopus)

Abstract

Perakine reductase (PR) is a novel member of the aldo-keto reductase enzyme superfamily from higher plants. PR from the plant Rauvolfia serpentina is involved in the biosynthesis of monoterpenoid indole alkaloids by performing NADPH-dependent reduction of perakine, yielding raucaffrinoline. However, PR can also reduce cinnamic aldehyde and some of its derivatives. After heterologous expression of a triple mutant of PR in Escherichia coli, crystals of the purified and methylated enzyme were obtained by the hanging-drop vapour-diffusion technique at 293 K with 100 mM sodium citrate pH 5.6 and 27% PEG 4000 as precipitant. Crystals belong to space group C222₁ and diffract to 2.0 Å, with unit-cell parameters a = 58.9, b = 93.0, c = 143.4 Å.

Original language	English
Pages (from-to)	1286-1289
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	62
Issue number	12
DOIs	https://doi.org/10.1107/S174430910605041X
Publication status	Published - Dec 2006
Externally published	Yes

Keywords

Biosynthesis
Indole alkaloid metabolism
Perakine reductase
Rauvolfia serpentina

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10.1107/S174430910605041X

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Rosenthal, C., Mueller, U., Panjikar, S., Sun, L., Ruppert, M., Zhao, Y., & Stöckigt, J. (2006). Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 62(12), 1286-1289. https://doi.org/10.1107/S174430910605041X

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title = "Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants",

abstract = "Perakine reductase (PR) is a novel member of the aldo-keto reductase enzyme superfamily from higher plants. PR from the plant Rauvolfia serpentina is involved in the biosynthesis of monoterpenoid indole alkaloids by performing NADPH-dependent reduction of perakine, yielding raucaffrinoline. However, PR can also reduce cinnamic aldehyde and some of its derivatives. After heterologous expression of a triple mutant of PR in Escherichia coli, crystals of the purified and methylated enzyme were obtained by the hanging-drop vapour-diffusion technique at 293 K with 100 mM sodium citrate pH 5.6 and 27\% PEG 4000 as precipitant. Crystals belong to space group C2221 and diffract to 2.0 {\AA}, with unit-cell parameters a = 58.9, b = 93.0, c = 143.4 {\AA}.",

keywords = "Biosynthesis, Indole alkaloid metabolism, Perakine reductase, Rauvolfia serpentina",

author = "Cindy Rosenthal and Uwe Mueller and Santosh Panjikar and Lianli Sun and Martin Ruppert and Yu Zhao and Joachim St{\"o}ckigt",

year = "2006",

month = dec,

doi = "10.1107/S174430910605041X",

language = "English",

volume = "62",

pages = "1286--1289",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

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Rosenthal, C, Mueller, U, Panjikar, S, Sun, L, Ruppert, M, Zhao, Y & Stöckigt, J 2006, 'Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 62, no. 12, pp. 1286-1289. https://doi.org/10.1107/S174430910605041X

Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants. / Rosenthal, Cindy; Mueller, Uwe; Panjikar, Santosh et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 62, No. 12, 12.2006, p. 1286-1289.

Research output: Contribution to journal › Article › Research › peer-review

TY - JOUR

T1 - Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants

AU - Rosenthal, Cindy

AU - Mueller, Uwe

AU - Panjikar, Santosh

AU - Sun, Lianli

AU - Ruppert, Martin

AU - Zhao, Yu

AU - Stöckigt, Joachim

PY - 2006/12

Y1 - 2006/12

N2 - Perakine reductase (PR) is a novel member of the aldo-keto reductase enzyme superfamily from higher plants. PR from the plant Rauvolfia serpentina is involved in the biosynthesis of monoterpenoid indole alkaloids by performing NADPH-dependent reduction of perakine, yielding raucaffrinoline. However, PR can also reduce cinnamic aldehyde and some of its derivatives. After heterologous expression of a triple mutant of PR in Escherichia coli, crystals of the purified and methylated enzyme were obtained by the hanging-drop vapour-diffusion technique at 293 K with 100 mM sodium citrate pH 5.6 and 27% PEG 4000 as precipitant. Crystals belong to space group C2221 and diffract to 2.0 Å, with unit-cell parameters a = 58.9, b = 93.0, c = 143.4 Å.

AB - Perakine reductase (PR) is a novel member of the aldo-keto reductase enzyme superfamily from higher plants. PR from the plant Rauvolfia serpentina is involved in the biosynthesis of monoterpenoid indole alkaloids by performing NADPH-dependent reduction of perakine, yielding raucaffrinoline. However, PR can also reduce cinnamic aldehyde and some of its derivatives. After heterologous expression of a triple mutant of PR in Escherichia coli, crystals of the purified and methylated enzyme were obtained by the hanging-drop vapour-diffusion technique at 293 K with 100 mM sodium citrate pH 5.6 and 27% PEG 4000 as precipitant. Crystals belong to space group C2221 and diffract to 2.0 Å, with unit-cell parameters a = 58.9, b = 93.0, c = 143.4 Å.

KW - Biosynthesis

KW - Indole alkaloid metabolism

KW - Perakine reductase

KW - Rauvolfia serpentina

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DO - 10.1107/S174430910605041X

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SN - 1744-3091

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JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

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ER -

Rosenthal C, Mueller U, Panjikar S, Sun L, Ruppert M, Zhao Y et al. Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2006 Dec;62(12):1286-1289. doi: 10.1107/S174430910605041X

Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants

Abstract

Keywords

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