Amino Acid-Catalyzed Conversion of Citral:  cis−trans Isomerization and Its Conversion into 6-Methyl-5-hepten-2-one and Acetaldehyde

Wolken, Wout A. M.; Have, Rimko ten; Werf, M.J. van der

doi:10.1021/jf0007378

Cited by 59 publications

(44 citation statements)

References 9 publications

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“…www.eurjoc.org13b, although it appeared to be a slow substrate (c max 16,21, and 43 % with OYE-1, OYE-2 and Zymomonas NCRreductase, respectively). OYE-3 was clearly the best enzyme (c 82 %, Table 2, Entries 5-8).…”

Section: Resultsmentioning

confidence: 98%

“…These variations in stereoselectivities can be explained by in situ (nonspecific) enzymatic (E/Z) isomerization of citral (1a). [21] As OYEs 1-3 are known to produce (R)-and (S)-1b from (E) and (Z) isomers of citral (1a), respectively, [8] the relative rate of competing (fast) C=C-bond reduction versus (slow) (E/Z) isomerization determines the overall outcome of the process (Scheme 2). Short reaction times furnish high stereoselectivities (but low conversion), whereas extended exposure times result in reduced ee values (but enhanced yields) of 1b.…”

Section: Resultsmentioning

confidence: 99%

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Asymmetric Bioreduction of Activated C=C Bonds Using Zymomonas mobilis NCR Enoate Reductase and Old Yellow Enzymes OYE 1–3 from Yeasts

Hall

Stueckler

Hauer³

et al. 2008

Eur J Org Chem

175

160

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The asymmetric bioreduction of C=C-bonds bearing an electron-withdrawing group, such as an aldehyde, ketone, imide, nitro, carboxylic acid, or ester moiety by a novel enoate reductase from Zymomonas mobilis and Old Yellow Enzymes OYE 1-3 from yeasts furnished the corresponding saturated products in up to Ͼ99 % ee. Depending on the substrate type, stereocontrol was achieved by variation of the substrate

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Section: Resultsmentioning

confidence: 98%

Section: Resultsmentioning

confidence: 99%

Asymmetric Bioreduction of Activated C=C Bonds Using Zymomonas mobilis NCR Enoate Reductase and Old Yellow Enzymes OYE 1–3 from Yeasts

Hall

Stueckler

Hauer³

et al. 2008

Eur J Org Chem

175

160

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“…Geranial and neral are trans-and cis-isomers, and are transformed into each other by keto-enol tautomerization, which is accelerated at alkaline or acidic condition (Kimura et al 1982;Wolken et al 2000). Therefore, citral is usually composed of a mixture of approximately 60% geranial and 40% neral.…”

Section: Discussionmentioning

confidence: 99%

Biosynthesis of geranial, a potent aroma compound in ginger rhizome (Zingiber officinale): Molecular cloning and characterization of geraniol dehydrogenase

Iijima

Koeduka

Suzuki

et al. 2014

Plant Biotechnology

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Fresh ginger (Zingiber officinale) rhizome is characterized by a pleasant citrus aroma and pungent flavor. The majority of the aroma-contributing volatiles are monoterpenoids, especially geraniol derivatives such as geranial, geranyl acetate, geraniol and citronellol. In this study, we investigated the interconversion of geraniol derivatives by incorporation experiments using deuterium-labeled geraniol and geranyl acetate. GC-MS analysis revealed that the incorporated geraniol and geranyl acetate were transformed and detected as geranial, geraniol, geranyl acetate and citronellol; however, nerol and neral were hardly detected. Next, we isolated and characterized a cDNA encoding geraniol dehydrogenase (ZoGeDH) by expressed sequence tag database mining. Phylogenic analysis of ZoGeDH resulted in its categorization into the cinnamyl alcohol dehydrogenase (CAD) group, along with the previously reported GeDHs of sweet basil (Ocimum basilicum) and wild perilla (P. setoyensis, P. citriodora, and P. frutescens). The recombinant ZoGeDH catalyzed the NADP-dependent oxidation from geraniol to citral. Furthermore, its substrate specificity was the highest for geraniol and nerol, while that for cinnamyl alcohol was 32% of the activity observed for geraniol. The expression levels of ZoGeDH in various ginger plant tissues were in accordance with the accumulation of geranial, except in old rhizome.

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“…Moreover, the isomerization remained constant after 6 h. Under alkaline conditions in Gly-NaOH buffer (pH 9.0-10.0), an equilibrium ratio between E/Z-isomers was reached an approximate ratio of 3:2. Isomerization of citral could be explained by Wolken et al (2010). In the presence of glycine, and especially under alkaline conditions, the isomerization was probably catalyzed via transient Schiff 's base formation between the aldehyde and glycine.…”

Section: Influence Factor On Enantioselectivity Of Oye2p Toward Citralmentioning

confidence: 99%

Identification of a yeast old yellow enzyme for highly enantioselective reduction of citral isomers to (R)-citronellal

Zheng

Lin

Zhang

et al. 2018

Bioresour. Bioprocess.

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Background: A NAD(P)H-dependent enoate reductase (OYE2p) from Saccharomyces cerevisiae YJM1341 was discovered by genome data mining for asymmetric reduction of (E/Z)-citral to (R)-citronellal with high enantioselectivity. Methods:This enzyme was heterologously expressed in E. coli and characterized for its biocatalytic properties. OYE2p was identified with reduction activities toward a diverse range of ɑ,β-unsaturated compounds bearing conjugated aldehyde, ketone, imide, carboxylic acid and ester.Results: OYE2p showed the highest specific activity at 40 °C and a pH optimum at 7.0-8.0. The stability of OYE2p was rather pH-independent, and the half-life time values of the enzyme at pH 6.0-8.0 were more than 257 h. With regard to the reduction of (E)-citral and (Z)-citral, OYE2p exhibited different selectivity patterns. (E)-citral was exclusively reduced to (R)-citronellal by OYE2p in ≥ 99% ee, which was independent on pH. OYE2p produced both enantiomers of citronellal from (Z)-citral, but showed (R)-citronellal formation tendency, and the ee value of (R)-citronellal was affected by pH in the reaction system. Accordingly, the ee values for (R)-citronellal formation increased with the increasing levels of E-isomer in the (E/Z)-citral mixture as well as the increase of pH. Under the reaction conditions (30 °C and pH 8.6), using purified OYE2p as catalyst, 200 mM (E/Z)-citral (an approximately 10:9 mixture of geometric E-isomer and Z-isomer) was efficiently converted to (R)-citronellal with 88.8% ee and 87.2% yield. Conclusion:All these positive features demonstrate high potential of OYE2p for practical synthesis of (R)-citronellal and in asymmetric reduction of activated alkenes.

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Amino Acid-Catalyzed Conversion of Citral: cis−trans Isomerization and Its Conversion into 6-Methyl-5-hepten-2-one and Acetaldehyde

Cited by 59 publications

References 9 publications

Asymmetric Bioreduction of Activated C=C Bonds Using Zymomonas mobilis NCR Enoate Reductase and Old Yellow Enzymes OYE 1–3 from Yeasts

Asymmetric Bioreduction of Activated C=C Bonds Using Zymomonas mobilis NCR Enoate Reductase and Old Yellow Enzymes OYE 1–3 from Yeasts

Biosynthesis of geranial, a potent aroma compound in ginger rhizome (<i>Zingiber officinale</i>): Molecular cloning and characterization of geraniol dehydrogenase

Identification of a yeast old yellow enzyme for highly enantioselective reduction of citral isomers to (R)-citronellal

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