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Literature summary for 1.1.1.317 extracted from

  • Rosenthal, C.; Mueller, U.; Panjikar, S.; Sun, L.; Ruppert, M.; Zhao, Y.; Stöckigt, J.
    Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants (2006), Acta Crystallogr. Sect. F, 62, 1286-1289.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
heterologous expression of a triple mutant (K98A/K242A/K294A) of perakine reductase in Escherichia coli Rauvolfia serpentina

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals of the purified and methylated enzyme are obtained by the hanging-drop vapour diffusion technique at 20°C 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 A, with unit-cell parameters a = 58.9, b = 93.0, c = 143.4 A Rauvolfia serpentina

Organism

Organism UniProt Comment Textmining
Rauvolfia serpentina Q3L181
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Purification (Commentary)

Purification (Comment) Organism
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Rauvolfia serpentina

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information probable dual functionality of perakine reductase, which may not only include alkaloid biosynthesis but may also include function in phenylpropanoid metabolism, generating cinnamic alcohols Rauvolfia serpentina ?
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