Crystal Structures of Pinoresinol-Lariciresinol and Phenylcoumaran Benzylic Ether Reductases and Their Relationship to Isoflavone Reductases

Min, Tongpil; Kasahara, Hiroyuki; Bedgar, Diana L.; Youn, BuHyun; Lawrence, Paulraj K.; Gang, David R.; Halls, Steven C.; Park, HaJeung; Hilsenbeck, Jacqueline L.; Davin, Laurence B.; Lewis, Norman G.; Kang, ChulHee

doi:10.1074/jbc.m308493200

Cited by 90 publications

(80 citation statements)

References 37 publications

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“…The crystal structure of the enzyme from Thuja plicata has been determined, and shows that the NADPH and substrate binding pockets are close enough for direct electron transfer to occur. The exact mechanism and reaction intermediates through which catalysis proceeds are still unknown due to the lack of published structures of enzymes with substrate bound [53].…”

Section: Ec 1231: Oxidoreductases Reducing Ceoec Groupmentioning

confidence: 99%

Review of NAD(P)H-dependent oxidoreductases: Properties, engineering and application

Vidal

Kelly

Mordaka

et al. 2018

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

213

138

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A B S T R A C T NAD(P)H-dependent oxidoreductases catalyze the reduction or oxidation of a substrate coupled to the oxidation or reduction, respectively, of a nicotinamide adenine dinucleotide cofactor NAD(P)H or NAD(P) + . NAD(P)Hdependent oxidoreductases catalyze a large variety of reactions and play a pivotal role in many central metabolic pathways. Due to the high activity, regiospecificity and stereospecificity with which they catalyze redox reactions, they have been used as key components in a wide range of applications, including substrate utilization, the synthesis of chemicals, biodegradation and detoxification. There is great interest in tailoring NAD(P)H-dependent oxidoreductases to make them more suitable for particular applications. Here, we review the main properties and classes of NAD(P)H-dependent oxidoreductases, the types of reactions they catalyze, some of the main protein engineering techniques used to modify their properties and some interesting examples of their modification and application.

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Section: Ec 1231: Oxidoreductases Reducing Ceoec Groupmentioning

confidence: 99%

Review of NAD(P)H-dependent oxidoreductases: Properties, engineering and application

Vidal

Kelly

Mordaka

et al. 2018

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

213

138

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“…The last step of the phenylpropene eugenol biosynthesis is catalyzed by EUGENOL SYNTHASE (EGS), an NADPH-dependent reductase belonging to the PIP (for Pinoresinol-lariciresinol reductase, Isoflavone reductase, Phenylcoumaran benzylic ether reductase) family (Min et al, 2003). To date, only a small number of plant EGSs, such as ObEGS1 (from Ocimum basilicum; Koeduka et al, 2006), CbEGS1 and CbEGS2 (from Clarkia breweri), and PhEGS1 (from petunia; Koeduka et al, 2008), have been functionally characterized.…”

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confidence: 99%

An R2R3-MYB Transcription Factor Regulates Eugenol Production in Ripe Strawberry Fruit Receptacles

et al. 2015

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Eugenol is a volatile phenylpropanoid that contributes to flower and ripe fruit scent. In ripe strawberry (Fragaria 3 ananassa) fruit receptacles, eugenol is biosynthesized by eugenol synthase (FaEGS2). However, the transcriptional regulation of this process is still unknown. We have identified and functionally characterized an R2R3 MYB transcription factor (EMISSION OF BENZENOID II [FaEOBII]) that seems to be the orthologous gene of PhEOBII from Petunia hybrida, which contributes to the regulation of eugenol biosynthesis in petals. The expression of FaEOBII was ripening related and fruit receptacle specific, although high expression values were also found in petals. This expression pattern of FaEOBII correlated with eugenol content in both fruit receptacle and petals. The expression of FaEOBII was repressed by auxins and activated by abscisic acid, in parallel to the ripening process. In ripe strawberry receptacles, where the expression of FaEOBII was silenced, the expression of CINNAMYL ALCOHOL DEHYDROGENASE1 and FaEGS2, two structural genes involved in eugenol production, was down-regulated. A subsequent decrease in eugenol content in ripe receptacles was also observed, confirming the involvement of FaEOBII in eugenol metabolism. Additionally, the expression of FaEOBII was under the control of FaMYB10, another R2R3 MYB transcription factor that regulates the early and late biosynthetic genes from the flavonoid/phenylpropanoid pathway. In parallel, the amount of eugenol in FaMYB10-silenced receptacles was also diminished. Taken together, these data indicate that FaEOBII plays a regulating role in the volatile phenylpropanoid pathway gene expression that gives rise to eugenol production in ripe strawberry receptacles.The octoploid cultivated strawberry (Fragaria 3 ananassa) is one of the most economically important, nonclimacteric, soft fruits, in which volatile compounds influence fruit flavor and aroma. Both characteristics contribute to the fruit organoleptic traits and are crucial factors to determine fruit quality.At present, extensive surveys on the components that contribute to strawberry flavor have been performed. In these studies, more than 360 volatiles have been identified (Latrasse, 1991;Nijssen, 1996;Zabetakis and Holden, 1997), but only 15 to 20 of them in wild varieties of strawberry are believed to be essential for sensory quality, together with nonvolatile sugars and organic acids (Schieberle and Hofmann, 1997). In contrast, in cultivated varieties of strawberry, only about six odor-active compounds have been identified as contributors to fruit flavor (Raab et al., 2006;Ulrich et al., 2007). Strawberry aroma is the result of the combined perception of fruity (ethyl butanoate, ethyl hexanoate, and methyl 2-methylbutanoat), green (Z-3-hexenal), sweaty (butanoic acid and 2-methylbutanoic acid), peach-like (g-decalactone), and caramel-like [4-hydroxy-2,5-dimethyl-3(2H)-furanone and 2,5-dimethyl-4-methoxy-3(2H)-furanone] flavor notes (Pyysalo et al., 1979;Larsen and Poll, 1992). Several wild strawb...

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“…Examples of these include pinoresinol/lariciresinol reductases (13,14), secoisolariciresinol dehydrogenase (15)(16)(17), phenylcoumaran benzylic ether reductase (14,18), isoflavone reductase (14), cinnamyl alcohol dehydrogenases (19,20), and chavicol/p-anol and eugenol/isoeugenol synthases (21,22), as well as dirigent proteins (in the presence of auxiliary oxidative capacity) (23)(24)(25). These studies are part of broader goals aimed toward (i) systematically engineering selected enzyme substrate binding pockets in terms of potentially modifying them to be more specific for a particular metabolite/metabolic pathway and (ii) better understanding how these pathways in plants have evolved.…”

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confidence: 99%

Mechanistic and Structural Studies of Apoform, Binary, and Ternary Complexes of the Arabidopsis Alkenal Double Bond Reductase At5g16970

Youn

Kim

Moinuddin

et al. 2006

Journal of Biological Chemistry

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In this study, we determined the crystal structures of the apoform, binary, and ternary complexes of the Arabidopsis alkenal double bond reductase encoded by At5g16970. This protein, one of 11 homologues in Arabidopsis thaliana, is most closely related to the Pinus taeda phenylpropenal double bond reductase, involved in, for example, heartwood formation. Both enzymes also have essential roles in plant defense, and can function by catalyzing the reduction of the 7-8-double bond of phenylpropanal substrates, such as p-coumaryl and coniferyl aldehydes in vitro. At5g16970 is also capable of reducing toxic substrates with the same alkenal functionality, such as 4-hydroxy-(2E)-nonenal. The overall fold of At5g16970 is similar to that of the zinc-independent medium chain dehydrogenase/reductase superfamily, the members of which have two domains and are dimeric in nature, i.e. in contrast to their original classification as being zinc-containing oxidoreductases. As provisionally anticipated from the kinetic data, the shape of the binding pocket can readily accommodate p-coumaryl aldehyde, coniferyl aldehyde, 4-hydroxy-(2E)-nonenal, and 2-alkenals. However, the enzyme kinetic data among these potential substrates differ, favoring p-coumaryl aldehyde. Tyr-260 is provisionally proposed to function as a general acid/base for hydride transfer. A catalytic mechanism for this reduction, and its applicability to related important detoxification mammalian proteins, is also proposed.

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Crystal Structures of Pinoresinol-Lariciresinol and Phenylcoumaran Benzylic Ether Reductases and Their Relationship to Isoflavone Reductases

Cited by 90 publications

References 37 publications

Review of NAD(P)H-dependent oxidoreductases: Properties, engineering and application

Review of NAD(P)H-dependent oxidoreductases: Properties, engineering and application

An R2R3-MYB Transcription Factor Regulates Eugenol Production in Ripe Strawberry Fruit Receptacles

Mechanistic and Structural Studies of Apoform, Binary, and Ternary Complexes of the Arabidopsis Alkenal Double Bond Reductase At5g16970

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