A molecular model for cinnamyl alcohol dehydrogenase, a plant aromatic alcohol dehydrogenase involved in lignification

McKie, James H.; Jaouhari, Rabih; Douglas, Kenneth T.; Goffner, Deborah; Feuillet, Catherine; Grima‐Pettenati, Jacqueline; Böudet, Alain M.; Baltas, Michel; Gorrichon, Liliane

doi:10.1016/0167-4838(93)90063-w

Cited by 51 publications

(42 citation statements)

References 37 publications

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“…This should be further investigated by examining the activities of truncated recombinant proteins. The NADH binding motif (GXGXXG) found in NADH-dependent enzymes such as lactate dehydrogenase (18), alcohol dehydrogenase (19), and hydrotransferase (20) was found in the deduced amino acid sequences of these two genes (Fig. 6, underlined).…”

Section: Resultsmentioning

confidence: 99%

Molecular Cloning and Characterization of the Gene Coding for Azoreductase from Bacillus sp. OY1-2 Isolated from Soil

Suzuki¹,

Yoda²,

Amin³

et al. 2001

Journal of Biological Chemistry

157

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Azo dyes are regarded as pollutants because they are not readily reduced under aerobic conditions. Bacillus sp. OY1-2 transforms azo dyes into colorless compounds, and this reduction is mediated by a reductase activity for the azo group in the presence of NADPH. A 1.2-kbp EcoRI fragment containing the gene that encodes azoreductase was cloned by screening the genomic library of Bacillus sp. OY1-2 with digoxigenin-labeled probe designed from the N-terminal amino acid sequence of the purified enzyme. An open reading frame encoding the azoreductase, consisting of 178 amino acids, was predicted from the nucleotide sequence. In addition, because only a Bacillus subtillis hypothetical protein was discovered in the public databases (with an amino acid identity of 52.8%), the gene encoding the azoreductase cloned in this study was predicted to be a member of a novel family of reductases. Southern blot analysis revealed that the azoreductase gene exists as a single copy gene on a chromosome. Escherichia coli-expressing recombinant azoreductase gave a ten times greater reducing activity toward azo dyes than the original Bacillus sp. OY1-2. In addition, the expressed azoreductase purified from the recombinant E. coli lysate by Red-Sepharose affinity chromatography showed a similar activity and specificity as the native enzyme. This is the first report describing the sequencing and characterization of a gene encoding the azo dye-reducing enzyme, azoreductase, from aerobic bacteria and its expression in E. coli.

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Section: Resultsmentioning

confidence: 99%

Molecular Cloning and Characterization of the Gene Coding for Azoreductase from Bacillus sp. OY1-2 Isolated from Soil

Suzuki¹,

Yoda²,

Amin³

et al. 2001

Journal of Biological Chemistry

157

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“…Quercetin belongs to the flavonoid class of aldose reductase inhibitors, many of which are also catechol derivatives. Flavones are widely distributed in the plant kingdom and flavones very similar to Quercetin containing catechol rings strongly inhibited cinnamyl ADH [37]. The inhibition of SDH may raise doubts about the osmotic theory of the etiology of diabetic complications, for it implies treatment by the inhibition of sorbitol production by aldose reductase and/or the lack of inhibition or, better, activation of sorbitol removal by SDH.…”

Section: Discussionmentioning

confidence: 99%

Inhibition and activation studies on sheep liver sorbitol dehydrogenase

Lindstad

Hermansen

McKinley-McKee

1994

European Journal of Biochemistry

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Reversible inhibition and activation, as well as protection against affinity labelling with DL-2-bromo-3-(5-imidazolyl)propionic acid, of sheep liver sorbitol dehydrogenase have been studied. The results presented are discussed in terms of enzyme active-site properties and may have potential applications for drug design.Kinetics with mainly sorbitol competitive inhibitors reveals that aliphatic thiols are generally the most potent inhibitors of enzyme activity. Inhibition and inactivation by heterocyclics parallel that seen previously with sorbitol dehydrogenase from other sources as well as with alcohol dehydrogenase from yeast. However, there are significant differences in relation to the structurally similar horse liver alcohol dehydrogenase, as the catalytic zinc of sorbitol dehydrogenase is more easily removed by chelating molecules. Several aldose reductase inhibitors are shown to also inhibit sorbito1 dehydrogenase, but at concentrations unlikely to be reached clinically. Enzyme activation has been observed with various compounds, in particular halo-alcohols and detergents.Several inhibitors provide competitive protection against enzyme inactivation by ~~-2 -b r o m o -3-(5-imidazolyl)propionic acid. This enables the dissociation constants for binary enzyme-inhibitor complexes to be determined. NADH protects noncompetitively against inactivation.The presence of some binary and ternary enzyme-NADH complexes is indicated from fluorescence emission spectra, as a shift in the fluorescence maximum and intensity is observed due to their formation.Sorbitol dehydrogenase (SDH) is present in various tissues [ l ] and is an important diagnostic marker for pathogenesis in the liver and testis [2-41. SDH catalyzes the reversible oxidation of several polyols to their corresponding ketoses with the concomitant reduction of NAD [l, 51: Polyol + NAD' + Ketose + NADH + H' Aldose reductase and sorbitol dehydrogenase constitute the sorbitol or polyol pathway, which catalyzes the conversion of glucose to fructose via sorbitol in vivo [l, 6, 71. In diabetes and galactosemia, high intracellular concentrations of aldoses causes the accumulation of the polyols sorbitol and galactitol. Since these molecules penetrate cell membranes poorly [8, 91, this results in hypertonicity of the tissue and osmotic complications. Polyol accumulation has been implicated in pathological changes in various tissues, includCorrespondence to J. S.

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“…The amino acid sequence of ZoGeDH showed 68%, 66%, and 49% identity with that of PcGeDH, ObGeDH, and ObCAD, respectively. ZoGeDH showed conserved NADP-and Zn1-binding domain motifs, and a Zn2 structural motif similar to other plant CADs and GeDHs (McKie et al 1993;Ragamustari et al 2013). BLAST search for ZoGeDH using GenBank showed the highest similarity with a predicted mannitol dehydrogenase in Phoenix dactylifera (79%, XP_008809345).…”

Section: Cloning and Phylogenetic Analysis Of Gedhmentioning

confidence: 96%

Biosynthesis of geranial, a potent aroma compound in ginger rhizome (<i>Zingiber officinale</i>): 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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A molecular model for cinnamyl alcohol dehydrogenase, a plant aromatic alcohol dehydrogenase involved in lignification

Cited by 51 publications

References 37 publications

Molecular Cloning and Characterization of the Gene Coding for Azoreductase from Bacillus sp. OY1-2 Isolated from Soil

Molecular Cloning and Characterization of the Gene Coding for Azoreductase from Bacillus sp. OY1-2 Isolated from Soil

Inhibition and activation studies on sheep liver sorbitol dehydrogenase

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

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